DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-3, 5-12, 14-19 and 21-23 are pending in this application and are being examined on the merits.
Applicant’s amendment to the claims filed 08/07/2026 is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s amendment to the specification filed 08/07/2026 is acknowledged.
Applicant’s amendment to the drawings filed 08/07/2026 is acknowledged.
Applicant’s remarks filed on 08/07/2026 in response to the non-final rejection mailed on 05/21/2026 are acknowledged and have been fully considered.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Objections to Specification
The objections to the disclosure are withdrawn in view of the amendments to address the use of trademarks, to remove of embedded hyperlinks, and to describe the Sequence Listing.
Objections to Drawings
The objections to the drawings are withdrawn in view of the amendment to reference the amino acid sequences shown in Figures 11-15 with sequence identifiers in accordance with 37 CFR 1.831.b, 37 CFR 1.831.c, and 37 CFR 1.832.a
Claim Objections
The objections to claims 5, 6, 12 and 22 are withdrawn in view of the instant claim amendments.
Claim Rejections - 35 USC § 112(b)
The rejection of claims 1-3, 5-12, 15-19 and 21-23 under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention are withdrawn in view of
the amendments to claims 1-3 to each recite “a catalytic triad Ser-Asp-His comprising the amino acids Ser97, Asp221, and His249 corresponding to SEQ ID NO: 2 for comparison”, “Gly99, Pro126, and Gly218 corresponding to SEQ ID NO: 2 for comparison”,
the amendments to claims 5-7 and 22-23 to each recite the Markush language of “selected from the group consisting of” followed by a group of alternatives,
the amendment to claim 11 to no longer recite exemplary claim language, and
the amendment to claim 15 to recite “a cell”.
Claims 1-3, 5-12, 14-19 and 21-23 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
The instant rejection is maintained from the previous Office action, and any newly recited portion is necessitated by claim amendment.
Claims 1 (claims 2-3, 5-12, 14-19 and 21-23 dependent therefrom) and 14 are indefinite for the phrases “wherein the enzyme or fragment thereof … is genetically modified” in claim 1 and “compared to a corresponding genetically unmodified enzyme or fragment thereof” in claim 14. The comparison of the enzyme recited in claims 1 and 14 to a genetically unmodified enzyme is unclear, as there are no recited genetic modifications in claims 1 and 14.
Response to Remarks: Beginning on page 17 of Applicant’s response to rejections under 35 USC 112(b); Applicant in summary contends the amendment to recite “genetically unmodified enzyme” overcomes the rejection as claim 1 recites a genetically modified enzyme.
Applicant’s remarks are considered and found not convincing, as there are no recited genetic modifications to the enzyme in claim 1.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 6 and 22 are rejected under 35 U.S.C. 112(d) as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
The instant rejection is newly stated and necessitated by claim amendment.
Claim 6 recites the isolated enzyme of fragment thereof of claim 2, wherein the isolated enzyme of fragment thereof shares at least 20% … sequence identity with SEQ ID NO: 2, 4, 6 or 8, and wherein the enzyme originates from a recited group of alternative organisms, while claim 2 recites the isolated enzyme of fragment thereof shares at least 20% identity with SEQ ID NOs: 2, 4, 6 or 8. As the origin of the enzyme does not structurally limit the recited enzyme, claim 6 does not further limit claim 2 from which it depends.
Claim 22 recites the enzyme of claim 3, wherein the enzyme shares at least 20% … sequence identity with SEQ ID NO: 2, 4, 6 or 8, and wherein the enzyme originates from a recited group of alternative organisms, while claim 3 recites the enzyme shares at least 20% identity with SEQ ID NOs: 2, 4, 6 or 8. As the origin of the enzyme does not structurally limit the recited enzyme, claim 22 does not further limit claim 3 from which it depends.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 112(a)
Claim Interpretation:
Claim 1 (claims 5, 7-8, 12, 14-16 dependent therefrom) is drawn to a method of degrading a polyolefin comprising providing a material comprising a polyolefin and an enzyme or fragment thereof capable of degrading the polyolefin, and allowing said enzyme or fragment thereof to degrade the polyolefin, wherein the enzyme or fragment thereof comprises a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 for numbering, and wherein the enzyme is genetically modified. The claims recite a genus of polypeptides, and except for the amino acids Ser97, Asp221, His249, Gly99, Pro126, and Gly218, the polypeptides are only required to share 20% identity with SEQ ID NOs 2, 4, 6 or 8. Therefore, the genus of recited polypeptides encompasses species that are considered to be widely variant with respect to sequence. Additionally, as SEQ ID NOs: 2, 4, 6 and 8 comprise 269, 274, 260 and 264 amino acids, respectively, the polypeptides recited in the claims are only required to have approximately 27 amino acids of the recited SEQ ID NOs in addition to the 6 specifically recited Ser97, Asp221, His249, Gly99, Pro126, and Gly218. Otherwise, the remainder of the amino acid sequences of the claimed polypeptides are considered to be unlimited.
Claim 2 (claims 6, 9, 11, 18-19, 21 and 23 dependent therefrom) is drawn to an isolate enzyme or fragment thereof comprising a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 for numbering, wherein the enzyme or fragment thereof capable of degrading the polyolefin and wherein the enzyme is genetically modified. The claims recite a genus of polypeptides, and except for the amino acids Ser97, Asp221, His249, Gly99, Pro126, and Gly218, the genus of polypeptides is only required to share 20% identity with SEQ ID NOs 2, 4, 6 or 8. Therefore, the genus of recited polypeptides encompasses species that are considered to be widely variant with respect to sequence. Additionally, as SEQ ID NOs: 2, 4, 6 and 8 comprise 269, 274, 260 and 264 amino acids, respectively, the polypeptides recited in the claims are only required to have approximately 27 amino acids of the recited SEQ ID NOs in addition to the 6 specifically recited Ser97, Asp221, His249, Gly99, Pro126, and Gly218. Otherwise, the remainder of the amino acid sequences of the claimed polypeptides are considered to be unlimited.
Claim 3 (claims 7, 10, 17 and 22 dependent therefrom) is drawn to a microorganism or host cell comprising an enzyme or fragment thereof comprising a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 for numbering, wherein the enzyme or fragment thereof capable of degrading the polyolefin and wherein the enzyme is genetically modified. The claims recite a genus of polypeptides, and except for the amino acids Ser97, Asp221, His249, Gly99, Pro126, and Gly218, the genus of polypeptides is only required to share 20% identity with SEQ ID NOs 2, 4, 6 or 8. Therefore, the genus of recited polypeptides encompasses species that are considered to be widely variant with respect to sequence. Additionally, as SEQ ID NOs: 2, 4, 6 and 8 comprise 269, 274, 260 and 264 amino acids, respectively, the polypeptides recited in the claims are only required to have approximately 27 amino acids of the recited SEQ ID NOs in addition to the 6 specifically recited Ser97, Asp221, His249, Gly99, Pro126, and Gly218. Otherwise, the remainder of the amino acid sequences of the claimed polypeptides are considered to be unlimited.
A. Claims 1-3, 5-12, 14-19 and 21-23 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor at the time the application was filed, had possession of the claimed invention.
The instant rejection is maintained from the previous Office action, and any newly recited portion is necessitated by claim amendment.
MPEP 2163.II.A.2.(a).i) states, “Whether the specification shows that applicant was in possession of the claimed invention is not a single, simple determination, but rather is a factual determination reached by considering a number of factors. Factors to be considered in determining whether there is sufficient evidence of possession include the level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention”.
For claims drawn to a genus, MPEP § 2163 states the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
According to MPEP 2163.II.A.3.(a).ii), [s]atisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’"
The factors considered in the Written Description requirement are (1) level of skill and knowledge in the art, (2) partial structure, (3) physical and/or chemical properties, (4) functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the (5) method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient." MPEP § 2163.
The claims recite (in relevant part) a genus of polypeptides capable of degrading polyolefin and comprising the catalytic triad Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 presented in SEQ ID NO: 2. As stated above, with the exception of the recited catalytic triad, the remaining amino acid sequences of the genus of polypeptides are unlimited. In this case, the genus of recited polypeptides encompasses species that are considered to be widely variant with respect to sequence.
The specification discloses the following representative species of the genus of recited polypeptides:
Bacillus cereus chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 2,
Bacillus flexus chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 4,
Bacillus licheniformis chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 6, and
Rhodococcus ruber chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 8.
Regarding the level of skill and knowledge in the art of amino acid modification, the reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached Form PTO-892) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see p. 7, column 1, top). Also, the unpredictability associated with residue substitution is exemplified by the reference of Zhang et al. (Structure 26:1474-1485, 2018; cited on the attached Form PTO-892), which discloses that even a substitution of a surface residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1).
In view of the high level of unpredictability in the art of amino acid modification, because the genus of polypeptides is widely variant with respect to structure, and the specification discloses the actual reduction to practice of only four species among a widely variant genus, one of skill in the art would reasonably conclude that the disclosure fails to provide a representative number of species to describe the genus, and thus, that the applicant was not in possession of the recited genus of non-naturally occurring polypeptides. The claimed subject matter is not supported by an adequate written description because a representative number of species has not been described.
B. Claims 1-3, 5-12, 14-19 and 21-23 are rejected under 35 U.S.C. 112(a) because the specification, while being enabling for an enzyme capable of degrading polyolefin comprising the amino acid sequence of SEQ ID NO: 2, 4, 6, or 8, does not reasonably provide enablement for all polypeptides having Ser97, Asp221, His249, Gly99, Pro126, and Gly218 corresponding to SEQ ID NO: 2 for numbering and sharing at least 20% identity with SEQ ID NOs: 2, 4, 6 or 8 as encompassed by the claims. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
The instant rejection is maintained from the previous Office action, and any newly recited portion is necessitated by claim amendment.
“The test of enablement is not whether any experimentation is necessary, but whether, if experimentation is necessary, it is undue.” In re Angstadt, 537 F.2d 498, 504, 190 USPQ 214, 219 (CCPA 1976). Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)) as follows: (A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. See MPEP § 2164.01(a). The Factors considered to be most relevant to the instant rejection are addressed in detail below.
The nature of the invention: According to the specification at page 2, lines 23-30, “The present invention provides methods and tools which enable biotechnological degradation of polyolefins … the present invention can overcome the problems of the prior art including but not limited to ineffective or slow biotechnical degradation of polyolefin polymers … the specific enzyme or microorganism of the present invention enable degradation methods at low temperature … indicating low energy need and costs”. The object of the invention is therefore to provide an efficient and effective method for enzymatic degradation of polyolefins.
The breadth of the claims: The claims recite (in relevant part) an enzyme or fragment thereof capable of degrading polyolefin and comprising Ser97, Asp221, His249, Gly99, Pro126, and Gly218 corresponding to SEQ ID NO: 2 for numbering and sharing at least 20% identity with SEQ ID NOs: 2, 4, 6 or 8. As stated above, with the exception of the recited amino acids and 20% identity to the recited SEQ ID NOs corresponding to approximately 27 amino acids of the recited SEQ ID NOs, the remaining amino acid sequences of the enzymes or fragments thereof are unlimited.
The state of the prior art; The level of one of ordinary skill; and The level of predictability in the art: According to MPEP 2164.03, “…what is known in the art provides evidence as to the question of predictability” and “[I]f one skilled in the art cannot readily anticipate the effect of a change within the subject matter to which that claimed invention pertains, then there is lack of predictability in the art.”
As noted above, other than the recited amino acids of the catalytic triad, the amino acid sequence of the recited enzymes or fragments thereof are unlimited. The reference of Singh (supra) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see p. 7, column 1, top).
The unpredictability associated with amino acid modification is exemplified by the reference of Zhang (supra) which discloses that even a mutation that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1).
As such, one of skill in the art would recognize a high level of unpredictability that all enzymes or fragments thereof comprising Ser97, Asp221, His249, Gly99, Pro126, and Gly218 corresponding to SEQ ID NO: 2 for numbering and sharing at least 20% identity with SEQ ID NOs: 2, 4, 6 or 8 as encompassed by the claims would maintain the desired activity/utility of polyolefin degradation.
The amount of direction provided by the inventor and The existence of working examples: The specification discloses the following working examples of an enzyme or fragment thereof capable of degrading polyolefin:
Bacillus cereus chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 2,
Bacillus flexus chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 4,
Bacillus licheniformis chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 6, and
Rhodococcus ruber chloroperoxidase comprising the amino acid sequence of SEQ ID NO: 8.
Other than these working examples, the specification fails to disclose any other enzyme or fragment thereof. Also, the specification fails to provide guidance for using those enzymes or fragments thereof that are non-functional or have activity other than the expected polyolefin degrading activity.
The quantity of experimentation needed to make or use the invention based on the content of the disclosure: While methods of modifying the amino acid sequence of a polypeptide were known at the time of the invention, it was not routine in the art to make and determine a use for all enzymes and fragments thereof as recited by the claims.
In view of the overly broad scope of the claims, the lack of guidance and working examples provided in the specification, the high level of unpredictability, and the state of the prior art, undue experimentation would be necessary for a skilled artisan to make and use the entire scope of the claimed invention. Applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of having the desired biological characteristics is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Response to Remarks: beginning on page 18 of Applicant’s response to rejections under 35 USC 112(a); Applicant in summary contends the specification provides adequate written description such that one of ordinary skill in the art would recognize the inventors were in possession of the claimed invention, and that the amended claims recite the enzyme has 20% sequence identity with SEQ ID NOs: 2, 4, 6 or 8; Applicant further contends there is no undue experimentation required to make and use the full scope of the claims, and that specification does not need to describe how to make and use every single embodiment within a claimed class as long as there is one method for making and using the claimed invention that bears a reasonable correlation to the entire scope of the claim; Applicant further contends the example of SEQ ID NOs 2, 4, 6 or 8, which only bear 22-46% identity with each other but comprise the recited amino acids, all are capable of degrading polyolefin.
Applicants remarks are considered and found not convincing.
Regarding written description, the species in the instant specification, referenced in the rejection above, which Applicant states conveys adequate written description of claimed genus of polypeptides, do not correspond to the structural variance of the genus recited in the claim of sharing at least 20% identity with SEQ ID NOs: 2, 4, 6 or 8. While Applicant states that the sequence identity relationship of these disclosed species ranges from 22-46% identity, such a statement does not correspond to the adequate description of the genus of polypeptides, particularly in view of the high level of unpredictability in the art of amino acid modification cited in the rejection above. Therefore one of skill in the art would reasonably conclude that the disclosure fails to provide a representative number of species to describe the genus, and thus, that the applicant was not in possession of the recited genus of polypeptides.
Regarding enablement, Applicant has not provided a method to make and use the claimed invention that bears a reasonable correlation to the entire scope of the claims, as the examples do not cover the full claim scope, and one of skill in the art would recognize a high level of unpredictability that all enzymes or fragments thereof comprising Ser97, Asp221, His249, Gly99, Pro126, and Gly218 corresponding to SEQ ID NO: 2 for numbering and sharing at least 20% identity with SEQ ID NOs: 2, 4, 6 or 8 as encompassed by the claims would maintain the desired activity/utility of polyolefin degradation. Additionally, there is no guidance for how to use those enzymes that do not have the expected activity. While Applicant states SEQ ID NOs 2, 4, 6 or 8 bear 22-46% identity with each other but comprise the recited amino acids, but all are capable of degrading polyolefin, this example does not apply to the entire scope of the claim, for while one of skill in the art would recognize that Applicant has disclosed 4 variant examples that show a desired activity, one of skill in the art would not expect this to be a universally reproducible trend throughout the entire scope of the claimed invention in view of the art disclosed in the rejection above.
Claim Rejections - 35 USC § 101
Claims 2-3, 6, 9-11, 17-18 and 21-23 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Applicant’s attention is directed to the "Guidance for Determining Subject Matter Eligibility Of Claims Reciting Or Involving Laws of Nature, Natural Phenomena, & Natural Products”, released on December 16, 2014.
The instant rejection is maintained from the previous Office action, and any newly recited portion is necessitated by claim amendment.
Claim Interpretation:
Claim 2 (claims 6, 9, 11, 18, 21 and 23 dependent therefrom) is drawn to an isolate enzyme or fragment thereof comprising a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 corresponding to the amino acids of SEQ ID NO: 2 for numbering, wherein the enzyme or fragment thereof capable of degrading the polyolefin and wherein the enzyme is genetically modified, and shares at least 20% sequence identity to SEQ ID NOs: 2, 4, 6 or 8. Regarding the limitation of “wherein the enzyme or fragment thereof … is genetically modified”, this limitation is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme of the claim) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims. Claim 6 further limits the sequence identity and the origin of the enzyme. Claims 9 and 11 limit the function of the enzyme. Claim 21 is drawn to a method of producing the enzyme of claim 2 wherein a host cell comprises a polynucleotide encoding the enzyme and expresses said enzyme. Claim 23 limits the enzyme class.
NCBI Accession No. WP_04290493.1 (1 page, 17 Feb 2015; cited on the attached Form PTO-892; herein referred to as NCBI1) discloses a hydrolase from Bacillus mycoides that shares 91.6% identity with SEQ ID NO: 2 and contains the amino acids Ser97, Asp221, His249, Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 [see Appendix A]. As the hydrolase of NCBI1 is encompassed by the structural limitations set forth in the claim, it is considered to have the functions recited in claims 2, 9 and 11, as the functions are considered inherent to the structure of the enzyme (MPEP 2112.I). As NCBI1 is derived from a RefSeq genome, it is considered to correspond to a polynucleotide encoding the enzyme. As NCBI1 discloses the enzyme is encoded in the genome of Bacillus mycoides, the enzyme is considered to be produced via expression from the polynucleotide encoding the enzyme. Given a broadest reasonable interpretation, claims 2, 6, 9, 11, 18, 21 and 23 encompass the naturally occurring product of the hydrolase of NCBI1, and a naturally occurring process of the production of the hydrolase of NCBI1 by Bacillus mycoides.
Claim 3 (claims 10, 17 and 22 dependent therefrom) is drawn to a microorganism or host cell comprising an enzyme or fragment thereof comprising a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 for numbering, wherein the enzyme or fragment thereof capable of degrading the polyolefin, wherein the enzyme is genetically modified, and wherein the enzyme has at least 20% sequence identity to SEQ ID NOs: 2, 4, 6 or 8. Regarding the limitation of “wherein the enzyme or fragment thereof … is genetically modified”, this limitation is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme of the claim) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims. Claim 10 limits the class of enzyme. Claim 17 limits the genus of the host cell. Claim 22 limits the enzyme to have at least 20% sequence identity to SEQ ID NOs: 2, 4, 6 or 8 and the origin of the enzyme.
As stated above, the hydrolase of NCBI1 contains the amino acids Ser97, Asp221, His249, Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 [see Appendix A] and originates from Bacillus mycoides. Regarding the capability of degrading polyolefin recited in claim 3, as the hydrolase of NCBI1 is encompassed by the structural limitations of the claim, it considered to have the capability of degrading polyolefin as the function of the enzyme is considered inherent to its structure (MPEP 2112.I). Given a broadest reasonable interpretation, claims 3, 7, 10, 17 and 22 encompass the naturally occurring product of the hydrolase of NCBI1, and a naturally occurring process of the production of the hydrolase of NCBI1 by Bacillus mycoides.
Claims 2, 6, 9, 11, 18, 21 and 23
Patent Eligibility Analysis Step 1: The claims are drawn to a composition of matter, which is one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claims recite a naturally occurring polypeptide, which is considered to be a law of nature or natural phenomena (a natural product). Accordingly, claims 2, 6, 9, 11, 18, 21 and 23 are directed to a judicial exception.
Patent Eligibility Analysis Step 2A Prong 2: Claim 2 recites the additional element that the enzyme is genetically modified. This additional element is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme of the claim) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims such that one of skill in the art would recognize the enzyme or fragment thereof as markedly different from its naturally occurring counterpart of the polypeptide of NCBI1.
There are no additional elements recited in claims 6, 9, 11, 18, 21 and 23 beyond the judicial exception.
Patent Eligibility Analysis Step 2B: The claims only recite the product of nature, without more and do not include any additional elements that could add significantly more to the judicial exception.
As such, the claims do not qualify as eligible subject matter. For these reasons the claim is rejected under section 101 as being directed to non-statutory subject matter.
Claims 3, 10, 17 and 22
Patent Eligibility Analysis Step 1: The claims are drawn to a composition of matter, which is one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claims recite a naturally occurring microorganism, which is considered to be a law of nature or natural phenomena (a natural product). Accordingly, claims 3, 10, 17 and 22 are directed to a judicial exception.
Patent Eligibility Analysis Step 2A Prong 2: Claim 3 recites the additional element that the enzyme is genetically modified. This additional element is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme of the claim) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims such that one of skill in the art would recognize the enzyme or fragment thereof as markedly different from its naturally occurring counterpart of the Bacillus mycoides cell comprising the polypeptide of NCBI1.
There are no additional elements recited in claims 10, 17 and 22 beyond the judicial exception.
Patent Eligibility Analysis Step 2B: The claims only recite the product of nature, without more and do not include any additional elements that could add significantly more to the judicial exception.
As such, the claims do not qualify as eligible subject matter. For these reasons the claim is rejected under section 101 as being directed to non-statutory subject matter.
Response to Remarks: beginning on page 22 of Applicants response to rejections under 35 USC 101; Applicant in summary contends the requirement for the claimed enzyme to be genetically modified precludes the subject matter from being a judicial exception.
Applicant’s remarks are considered and found not convincing. As discussed above, the limitation of “wherein the enzyme or fragment thereof … is genetically modified”, this limitation is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme or fragment thereof) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims such that one of skill in the art would recognize the enzyme or fragment thereof as markedly different from its naturally occurring counterpart.
Claim Rejections - 35 USC § 102
Claims 2, 6, 9, 11, 18 and 23 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Accession No. A0A161QNJ7_BACCE (1 page, 06 July 2016; cited on the IDS filed 10/10/2023; herein referred to as UNI1).
The instant rejection is maintained from a previous Office action, and any newly recited portion is necessitated by amendment.
Claim 2 (claims 6, 9, 11, 18 and 23 dependent therefrom) is drawn to an isolated enzyme or fragment thereof comprising a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 of SEQ ID NO: 2 for numbering,
wherein the enzyme or fragment thereof capable of degrading a polyolefin and
wherein the enzyme is genetically modified, and
wherein the enzyme or fragment thereof shares at least 20% sequence identity with SEQ ID NO: 2, 4, 6 or 8.
Claim 6 is drawn to the isolated enzyme or fragment thereof of claim 2, wherein the enzyme or fragment thereof has a least 20% sequence identity to SEQ ID NO: 2, 4, 6 or 8, and wherein the enzyme originates from or is an enzyme of a bacterium or fungus selected from the organisms listed in the claim.
Claim 9 is drawn to the isolated enzyme or fragment thereof of claim 2, wherein the isolated enzyme or fragment thereof is capable of degrading the polyolefin in the presence or absence of hydrogen peroxide at a temperature of at least 20 °C, at least 25 °C, at least 30 °C, at least 37 °C or at a temperature of 30 – 95 °C.
Claim 11 is drawn to the isolated enzyme or fragment thereof of claim 9, wherein the isolated enzyme or fragment thereof is capable of degrading the polyolefin in the presence of hydrogen peroxide and the hydrogen peroxide is produced by another enzyme, fragment, microorganism or host cell, or a microorganism or host cell comprising said superoxide dismutase.
Claim 18 is drawn to a polynucleotide encoding the enzyme of fragment thereof of claim 2.
Claim 23 is drawn to the enzyme or fragment thereof of claim 2, wherein the enzyme is selected from the group comprising or consisting of the enzyme class alternatives recited in the claim.
Regarding the limitation in claim 2 of “wherein the enzyme or fragment thereof … is genetically modified”, this limitation is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme of the claim) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims.
Regarding claims 2 and 6, UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has the amino acids Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
Regarding claim 9, the enzyme of UNI1 is considered have the capability of degrading the polyolefin in the presence or absence of hydrogen peroxide at a temperature of at least 20 °C, at least 25 °C, at least 30 °C, at least 37 °C or at a temperature of 30 – 95 °C, as the enzyme of UNI1 satisfies the structural limitations of the claims, and the function of the enzyme is presumed to be inherent to its structure (MPEP 2112.I).
Regarding claim 11, the enzyme of UNI1 is considered have the capability of degrading the polyolefin in the presence of hydrogen peroxide and the hydrogen peroxide, as the enzyme of UNI1 satisfies the structural limitations of the claims, and the function of the enzyme is presumed to be inherent to its structure (MPEP 2112.I). The limitations of claim 11 regarding the production of hydrogen peroxide by another in lines 4-6 do not structurally limit the enzyme of claim 11.
Regarding claim 18, as UNI1 discloses a chloroperoxidase from the naturally occurring Bacillus cereus, it is considered to be encoded by a polynucleotide.
Regarding claim 23, UNI1 discloses the non-heme chloroperoxidase from Bacillus cereus.
For these reasons, UNI1 anticipates claims 2, 6, 9, 11, 18 and 23.
Response to remarks: beginning on page 22 of Applicant’s response to rejections under 35 USC 102; Applicant in summary contends that UNI1 does not disclose a genetically modified enzyme as recited in the claims.
Applicants remarks are considered and found not convincing to overcome the rejection. The limitation in claim 2 of “wherein the enzyme or fragment thereof … is genetically modified”, this limitation is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme of the claim) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims. Therefore as described in the rejection above, the polypeptide of UNI1 satisfies the structural limitations of the enzyme of claim 2.
Claim Rejections - 35 USC § 103
Claims 1, 3, 5, 7-8, 10, 12, 14-17, 19 and 21-22 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2014/079844 (cited on the IDS filed 10/10/2023; herein referred to as Boisart) in view of UNI1 and evidentiary reference Rojas et al. (Polymer, 2008, 49:2985; cited on the attached Form PTO-892; herein Rojas).
The instant rejection is maintained from a previous Office action, and any newly recited portion is necessitated by amendment.
Claim 1 (claims 5, 7-8, 12, 14-16 dependent therefrom) is drawn to a method of degrading a polyolefin comprising
providing a material comprising a polyolefin and an enzyme or fragment thereof capable of degrading the polyolefin, and
allowing said enzyme or fragment thereof to degrade the polyolefin,
wherein the enzyme or fragment thereof comprises a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 for numbering,
wherein the enzyme is genetically modified, and
wherein the enzyme or fragment thereof shares at least 20% sequence identity with SEQ ID NO: 2, 4, 6 or 8.
Claim 3 (claims 10, 17 and 22 dependent therefrom) is drawn to a microorganism or host cell comprising an enzyme or fragment thereof comprising a catalytic triad of Ser-Asp-His corresponding to amino acids Ser97, Asp221, and His249 of SEQ ID NO: 2 for numbering, and the amino acids Gly99, Pro126 and Gly218 corresponding to SEQ ID NO: 2 for numbering,
wherein the enzyme or fragment thereof capable of degrading the polyolefin and
wherein the enzyme is genetically modified, and
wherein the enzyme or fragment thereof shares at least 20% sequence identity with SEQ ID NO: 2, 4, 6 or 8.
Claim 19 is drawn to an expression vector or plasmid comprising the polynucleotide of claim 18.
Claim 21 is drawn to a method of producing the enzyme or fragment thereof of claim 2, wherein a recombinant microorganism or host cell comprising the polynucleotide encoding the enzyme or fragment thereof is allowed to express said enzyme or fragment thereof.
Regarding the limitation of “wherein the enzyme or fragment thereof … is genetically modified” recited in claims 1 and 3, this limitation is considered a product-by-process limitation that is drawn to the method of making the enzyme or fragment thereof recited in the claim. According to MPEP 2113.I, the patentability of a product (e.g., the enzyme of the claim) does not depend on its method of production (e.g., genetic modification). As such the limitation of “genetically modified” does not structurally limit the enzyme of the claims.
Claims 1 and 3 will be discussed with their respective dependents when possible.
Boisart relates to methods for recycling plastic products [title] and discusses the use of enzymes to degrade polymers of plastic products [abstract].
Regarding claim 1, Boisart teaches a method of degrading polymers of plastic products [abstract] corresponding to degradation of polyolefins, comprising the degradation of polymer plastic products by at least one enzyme [p 3, lines 4-7], wherein the enzyme is considered to be capable of degrading polyolefin. Boisart teaches the enzyme is selected from cutinase, lipase, esterase, amidase, aryl-acylamidase, oligomer hydrolase, such as 6- aminohexanoate cyclic dimer hydrolase, 6-aminohexanoate dimer hydrolase, 6-aminohexanoate-oligomer hydrolase, peroxidase, and laccase [p 4, lines 9-14]. Boisart further teaches the degradation of plastic products that consist of polymers containing a main saturated linear carbon chain [p 9, lines 5-7], which corresponds to the polyolefin of polyethylene as evidenced by Figure 2 of Rojas which shows the linear saturated carbon chain polymer polyethylene.
Boisart does not teach that the enzyme comprises Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 for numbering, and wherein the enzyme or fragment thereof shares at least 20% sequence identity with SEQ ID NO: 2, 4, 6 or 8.
UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has the amino acids Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
In view of UNI1, it would have been prima facie obvious before the effective filing date for one of ordinary skill in the art to modify the method of Boisart by replacing the peroxidase enzyme with the chloroperoxidase of UNI1 to arrive at the claimed invention, since the simple substitution of one known element for another results in a predictable result. One of ordinary skill in the art would have recognized that the peroxidase enzyme of Boisart and the chloroperoxidase enzyme of UNI1 are both peroxidase enzymes, and as such both are capable of being incorporated into such methods as described by Boisart. Thus it would have been obvious to one of ordinary skill in the art to replace the peroxidase of Boisart with the chloroperoxidase of UNI1, as one of ordinary skill in the art would have been able to carry out such a substitution with a reasonable expectation of success because both Boisart and UNI1 relate to peroxidase enzymes.
Regarding claim 5 (dependent from claim 1), the enzyme of UNI1 shares 97.2% sequence identity with SEQ ID NO: 2 and is from Bacillus cereus [see Appendix B].
Regarding claim 7 (dependent from claim 1), the enzyme of UNI1 is a chloroperoxidase.
Regarding claim 8 (dependent from claim 1), Boisart teaches the plastic product comprises at least one polymer chosen among polyesters and polyamides such as polyethylene terephthalate and other polyesters and polyamides disclosed on [p 3, line 8 to p 4, line 4].
Regarding claim 12 (dependent from claim 1), as Boisart teaches degrading the plastic products such as polyethylene to monomers [abstract, p 3 lines 8-12], the method is considered to produce the monomer of an alkane.
Regarding claim 14 (dependent from claim 1), in view of the indefiniteness of the comparison to determine the increased polyolefin degradation as set forth in the rejection of 112(b) above, the enzyme of claim 14 encompasses any polyolefin degradation activity, and therefore the rejection of claim 14 can be included with the rejection of claim 1 above.
Additionally, as the enzyme of UNI1 is encompassed by the structural limitations of the enzyme in the claims, it is considered to have the increased ability to degrade polyolefin compared to a corresponding genetically unmodified enzyme or fragment thereof, as the function of the enzyme is considered inherent to its structure (MPEP 2112.I).
Regarding claim 15 (dependent from claim 1), the enzyme of UNI1 does not disclose a signal sequence, and is therefore considered to not comprise a detectable signal sequence and therefore is considered not to be secreted out of the cell which produces it.
Regarding claim 16 (dependent from claim 1), the limitation “wherein the enzyme or fragment thereof is encoded by a heterologous nucleotide sequence” does not structurally limit the enzyme used in the method of claim 1. Additionally, the phrase “heterologous nucleotide sequence” is considered a product-by-process limitation, as the origin of the nucleotide being heterologous and therefore the production of the nucleotide sequence does not impose any structural limitations on the product of the nucleotide sequence itself (MPEP 2113.I). As UNI1 discloses a chloroperoxidase from the naturally occurring Bacillus cereus, it is considered to be encoded by a nucleotide sequence.
Regarding claims 19 (dependent from claims 2 and 18) and 21 (dependent from claim 2), Boisart teaches the method of enzymatic polyolefin degradation as discussed in the rejection of claim 1 above comprising cloning a gene of interest for into a vector [p 19, lines 10-12] for expression of the encoded enzyme in the host cell E. coli [p 19, lines 1-2], and UNI1 teaches a non-heme chloroperoxidase from Bacillus cereus discussed in the rejection of claim 2 under 35 USC 102 above.
In view of Boisart and UNI1, it would have been prima facie obvious before the effective filing date for one of ordinary skill in the art to incorporate the polynucleotide encoding the enzyme of UNI1 into a vector for expression in a host cell, as taught by Boisart, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to incorporate the polynucleotide encoding the enzyme of UNI1 into a vector for expression because Boisart teaches the cloning and expression of enzymes capable of degrading polyolefins such as peroxidases to carry out the method of degrading polyolefins, and UNI1 teaches a peroxidase. One of ordinary skill in the art would have had a reasonable expectation of success because Boisart and UNI1 relate to peroxidases.
Regarding claim 3, Boisart teaches the method of enzymatic polyolefin degradation as discussed in the rejection of claim 1 above comprising cloning a gene of interest for into a vector [p 19, lines 10-12] for expression of the encoded enzyme in the host cell E. coli [p 19, lines 1-2], wherein the method can be carried out with enzymes that include peroxidase [p 4, lines 9-14], and UNI1 teaches a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has the amino acids Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
In view of Boisart and UNI1, it would have been prima facie obvious before the effective filing date for one of ordinary skill in the art to incorporate the polynucleotide encoding the enzyme of UNI1 into a vector for expression in a host cell, as taught by Boisart, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to incorporate the polynucleotide encoding the enzyme of UNI1 into a vector for expression because Boisart teaches the cloning and expression of enzymes capable of degrading polyolefins such as peroxidases to carry out the method of degrading polyolefins, and UNI1 teaches a peroxidase. One of ordinary skill in the art would have had a reasonable expectation of success because Boisart and UNI1 relate to peroxidases.
Regarding claim 10 (dependent from claim 3), the combined method of Boisart and UNI1 comprises a host cell described above that is considered to have the activity of being capable of degrading the polyolefin in the presence or absence of hydrogen peroxide at a temperature of at least 20 °C, at least 25 °C, at least 30 °C, at least 37 °C or at a temperature of 30 – 95 °C, as the host cell the combined method of Boisart and UNI1 satisfies the structural limitations of the claims, and the function of the cell is presumed to be inherent to its structure (MPEP 2112.I).
Regarding claim 17 (dependent from claim 3), Boisart teaches the host cell is E. coli [p 19, lines 1-2].
Regarding claim 22 (dependent from claim 3), the enzyme of UNI1 shares 97.2% sequence identity with SEQ ID NO: 2 and is from Bacillus cereus [see Appendix B].
Therefore, the invention of claims 1, 3, 5, 7-8, 10, 12, 14-17, 19 and 21-22 would have been obvious to one of ordinary skill in the art before the effective filing date.
Response to remarks: beginning on page 22 of Applicant’s response to rejections under 35 USC 103; Applicant in summary contends Boisart does not disclose the degradation of polyolefins; Applicant further contends Boisart does not specifically disclose using a chloroperoxidase, and therefore the proposed simple substitution of the rejection is not supported.
Applicant’s remarks are considered and found not convincing. While Boisart does not explicitly recite degradation of polyolefins, Boisart describes degrading plastics which are considered to encompass polyolefins. Additionally, Boisart teaches the degradation of plastic products that consist of polymers containing a main saturated linear carbon chain [p 9, lines 5-7], which corresponds to the polyolefin of polyethylene as evidenced by Figure 2 of Rojas which shows the linear saturated carbon chain polymer polyethylene. Furthermore, Boisart discloses different classes of enzymes that include peroxidases, and the polypeptide of UNI1 is a peroxidase. One of ordinary skill in the art would have recognized the peroxidase of Boisart and the chloroperoxidase of UNI1 are both peroxidases, and as such both are capable of being incorporated into the method of Boisart as described in the rejection above. While Applicant states Boisart discloses the use of a manganese peroxidase for use in the method that is not a chloroperoxidase, Boisart does not exclude the use of any particular peroxidase, and MPEP 2123.I states “the use of patents as references is not limited to what the patentees describe as their own inventions or to the problems with which they are concerned. They are part of the literature of the art, relevant for all they contain”. Additionally, MPEP2123.II states disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments. Therefore, one of ordinary skill in the art in making the substitution proposed in the rejection above to use the polypeptide of UNI1 with the method of Boisart based on the polypeptide of UNI1 being a peroxidase would arrive at the claimed invention.
Double Patenting
A. Claims 1-3, 5-12, 14-19 and 21-23 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/579070 (herein “reference application”) in view of Boisart, UNI1 and evidentiary reference Rojas.
The instant rejection is maintained from a previous Office action, and any newly recited portion is necessitated by amendment.
Instant claims 1, 2 and 3 will be discussed with their respective dependents when possible.
Regarding instant claim 1, claim 1 of the reference application recites a method of degrading a hydrocarbon chain comprising providing a material comprising a hydrocarbon chain and an enzyme of fragment thereof capable of degrading a polyolefin and allowing said enzyme to degrade the polyolefin.
The claims of the reference application do not recite the enzyme or fragment thereof comprising amino acids Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 for numbering, and >20% sequence identity with SEQ ID NOs: 2, 4, 6 or 8.
Boisart relates to methods for recycling plastic products [title] and discusses the use of enzymes to degrade polymers of plastic products [abstract].
Regarding instant claim 1, Boisart discloses a method of degrading polymers of plastic products [abstract] corresponding to degradation of polyolefins, comprising the degradation of polymer plastic products by at least one enzyme [p 3, lines 4-7], wherein the enzyme is considered to be capable of degrading polyolefin. Boisart discloses the enzyme is selected from cutinase, lipase, esterase, amidase, aryl-acylamidase, oligomer hydrolase, such as 6- aminohexanoate cyclic dimer hydrolase, 6-aminohexanoate dimer hydrolase, 6-aminohexanoate-oligomer hydrolase, peroxidase, and laccase [p 4, lines 9-14]. Boisart further discloses the degradation of plastic products that consist of polymers containing a main saturated linear carbon chain [p 9, lines 5-7], which corresponds to the polyolefin of polyethylene as evidenced by Figure 2 of Rojas which shows the linear saturated carbon chain polymer polyethylene.
UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 for numbering [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
In view of Boisart, it would have been obvious before the effective filing date for one of ordinary skill in the art to modify the claims of the reference application by using a peroxidase enzyme as disclosed by Boisart, and using the peroxidase enzyme of UNI1 to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the claims of the reference application by using a peroxidase enzyme because Boisart discloses peroxidase enzymes can be used to degrade polyolefins down to monomers. One of ordinary skill in the art would have had a reasonable expectation of success because the reference application and Boisart relate to enzymatic degradation of polyolefins.
In view of UNI1, it would have been obvious before the effective filing date for one of ordinary skill in the art to modify the combined method of the reference application and Boisart by replacing the peroxidase enzyme with the chloroperoxidase of UNI1, since the simple substitution of one known element for another results in a predictable result. One of ordinary skill in the art would have recognized that the peroxidase enzyme of Boisart and the chloroperoxidase enzyme of UNI1 are both peroxidase enzymes, and as such both are capable of being incorporated into such methods as described by Boisart. Thus it would have been obvious to one of ordinary skill in the art to replace the peroxidase of Boisart with the chloroperoxidase of UNI1, as one of ordinary skill in the art would have been able to carry out such a substitution with a reasonable expectation of success because both Boisart and UNI1 relate to peroxidase enzymes.
Regarding instant claim 5 (dependent from instant claim 1), the enzyme of UNI1 shares 97.2% sequence identity with SEQ ID NO: 2 and is from Bacillus cereus [see Appendix B].
Regarding instant claim 7 (dependent from instant claim 1), the enzyme of UNI1 is a chloroperoxidase.
Regarding instant claim 8 (dependent from instant claim 1), Boisart discloses the plastic product comprises at least one polymer chosen among polyesters and polyamides such as polyethylene terephthalate and other polyesters and polyamides disclosed on [p 3, line 8 to p 4, line 4].
Regarding instant claim 12 (dependent from instant claim 1), as Boisart discloses degrading the plastic products such as polyethylene to monomers [abstract, p 3 lines 8-12], the method is considered to produce the monomer of an alkane.
Regarding instant claim 14 (dependent from instant claim 1), as the enzyme of UNI1 is encompassed by the structural limitations of the enzyme in the claims, it is considered to have the increased ability to degrade polyolefin compared to a corresponding genetically unmodified enzyme or fragment thereof, as the function of the enzyme is considered inherent to its structure (MPEP 2112.I).
Regarding instant claim 15 (dependent from instant claim 1), the enzyme of UNI1 does not disclose a signal sequence, and is therefore considered to not comprise a signal sequence and therefore is considered not to be secreted out of the cell which produces it.
Regarding instant claim 16 (dependent from instant claim 1), the limitation “wherein the enzyme or fragment thereof is encoded by a heterologous nucleotide sequence” does not structurally limit the enzyme used in the method of instant claim 1. Additionally, the phrase “heterologous nucleotide sequence” is considered a product-by-process limitation, as the origin of the nucleotide being heterologous and therefore the production of the nucleotide sequence does not impose any structural limitations on the product of the nucleotide sequence itself (MPEP 2113.I). As UNI1 discloses a chloroperoxidase from the naturally occurring Bacillus cereus, it is considered to be encoded by a nucleotide sequence.
Regarding instant claims 2 and 6 (dependent from instant claim 2), UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 for numbering [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
Regarding instant claim 9 (dependent from instant claim 2), the enzyme of UNI1 is considered have the capability of degrading the polyolefin in the presence or absence of hydrogen peroxide at a temperature of at least 20 °C, at least 25 °C, at least 30 °C, at least 37 °C or at a temperature of 30 – 95 °C, as the enzyme of UNI1 satisfies the structural limitations of the claims, and the function of the enzyme is presumed to be inherent to its structure (MPEP 2112.I).
Regarding instant claim 11 (dependent from instant claim 9), the enzyme of UNI1 is considered have the capability of degrading the polyolefin in the presence of hydrogen peroxide and the hydrogen peroxide, as the enzyme of UNI1 satisfies the structural limitations of the claims, and the function of the enzyme is presumed to be inherent to its structure (MPEP 2112.I). The limitations of instant claim 11 regarding the production of hydrogen peroxide by another in lines 4-6 do not structurally limit the enzyme of instant claim 11.
Regarding instant claim 18 (dependent from instant claim 2), as UNI1 discloses a chloroperoxidase from the naturally occurring Bacillus cereus, it is considered to be encoded by a polynucleotide.
Regarding instant claims 19 (dependent from instant claim 18) and 21 (dependent from instant claim 2), Boisart discloses the method of enzymatic polyolefin degradation as discussed in the rejection of claim 1 above comprising cloning a gene of interest for into a vector [p 19, lines 10-12] for expression of the encoded enzyme in the host cell E. coli [p 19, lines 1-2], and UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus.
Regarding instant claim 23 (dependent from instant claim 2), UNI1 discloses the non-heme chloroperoxidase from Bacillus cereus.
Regarding instant claim 3, Boisart discloses the method of enzymatic polyolefin degradation as discussed in the rejection of instant claim 1 above comprising cloning a gene of interest for into a vector [p 19, lines 10-12] for expression of the encoded enzyme in the host cell E. coli [p 19, lines 1-2], wherein the method can be carried out with enzymes that include peroxidase [p 4, lines 9-14], and UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 for numbering [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
It would have been obvious before the effective filing date for one of ordinary skill in the art to modify the combined method of the reference application, Boisart and UNI1 by incorporating the polynucleotide encoding the enzyme of UNI1 into a vector for expression in a host cell, as taught by Boisart, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined method of the reference application, Boisart and UNI1 by incorporating the polynucleotide encoding the enzyme of UNI1 into a vector for expression because Boisart discloses the cloning and expression of enzymes capable of degrading polyolefins such as peroxidases to carry out the method of degrading polyolefins, and UNI1 discloses a peroxidase. One of ordinary skill in the art would have had a reasonable expectation of success because Boisart and UNI1 relate to peroxidases.
Regarding instant claim 10 (dependent from instant claim 3), the combined method of the reference application, Boisart and UNI1 comprises a host cell which is considered to have the activity of being capable of degrading the polyolefin in the presence or absence of hydrogen peroxide at a temperature of at least 20 °C, at least 25 °C, at least 30 °C, at least 37 °C or at a temperature of 30 – 95 °C, as the host cell from the combined method satisfies the structural limitations of the instant claims, and the function of the cell is presumed to be inherent to its structure (MPEP 2112.I).
Regarding instant claim 17 (dependent from instant claim 3), Boisart discloses the host cell is E. coli [p 19, lines 1-2].
Regarding instant claim 22 (dependent from instant claim 3), the enzyme of UNI1 shares 97.2% sequence identity with SEQ ID NO: 2 and is from Bacillus cereus [see Appendix B].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
B. Claims 1-3, 5-12, 14-19 and 21-23 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 19/102689 (herein “reference application”) in view of Boisart, UNI1 and evidentiary reference Rojas.
The instant rejection is maintained from a previous Office action, and any newly recited portion is necessitated by amendment.
Instant claims 1, 2 and 3 will be discussed with their respective dependents when possible.
Regarding instant claim 1, claim 1 of the reference application recites a method of degrading a polyolefin comprising providing a material comprising a polyolefin and an enzyme of fragment thereof capable of degrading a polyolefin and allowing said enzyme to degrade the polyolefin.
The claims of the reference application do not recite the enzyme or fragment thereof comprising amino acids Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 for numbering, and >20% sequence identity with SEQ ID NOs: 2, 4, 6 or 8.
Boisart relates to methods for recycling plastic products [title] and discusses the use of enzymes to degrade polymers of plastic products [abstract].
Regarding instant claim 1, Boisart discloses a method of degrading polymers of plastic products [abstract] corresponding to degradation of polyolefins, comprising the degradation of polymer plastic products by at least one enzyme [p 3, lines 4-7], wherein the enzyme is considered to be capable of degrading polyolefin. Boisart discloses the enzyme is selected from cutinase, lipase, esterase, amidase, aryl-acylamidase, oligomer hydrolase, such as 6- aminohexanoate cyclic dimer hydrolase, 6-aminohexanoate dimer hydrolase, 6-aminohexanoate-oligomer hydrolase, peroxidase, and laccase [p 4, lines 9-14]. Boisart further discloses the degradation of plastic products that consist of polymers containing a main saturated linear carbon chain [p 9, lines 5-7], which corresponds to the polyolefin of polyethylene as evidenced by Figure 2 of Rojas which shows the linear saturated carbon chain polymer polyethylene.
UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
In view of Boisart, it would have been obvious before the effective filing date for one of ordinary skill in the art to modify the claims of the reference application by using a peroxidase enzyme as disclosed by Boisart, and using the peroxidase enzyme of UNI1 to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the claims of the reference application by using a peroxidase enzyme because Boisart discloses peroxidase enzymes can be used to degrade polyolefins down to monomers. One of ordinary skill in the art would have had a reasonable expectation of success because the reference application and Boisart relate to enzymatic degradation of polyolefins.
In view of UNI1, it would have been obvious before the effective filing date for one of ordinary skill in the art to modify the combined method of the reference application and Boisart by replacing the peroxidase enzyme with the chloroperoxidase of UNI1, since the simple substitution of one known element for another results in a predictable result. One of ordinary skill in the art would have recognized that the peroxidase enzyme of Boisart and the chloroperoxidase enzyme of UNI1 are both peroxidase enzymes, and as such both are capable of being incorporated into such methods as described by Boisart. Thus it would have been obvious to one of ordinary skill in the art to replace the peroxidase of Boisart with the chloroperoxidase of UNI1, as one of ordinary skill in the art would have been able to carry out such a substitution with a reasonable expectation of success because both Boisart and UNI1 relate to peroxidase enzymes.
Regarding instant claim 5 (dependent from instant claim 1), the enzyme of UNI1 shares 97.2% sequence identity with SEQ ID NO: 2 and is from Bacillus cereus [see Appendix B].
Regarding instant claim 7 (dependent from instant claim 1), the enzyme of UNI1 is a chloroperoxidase.
Regarding instant claim 8 (dependent from instant claim 1), Boisart discloses the plastic product comprises at least one polymer chosen among polyesters and polyamides such as polyethylene terephthalate and other polyesters and polyamides disclosed on [p 3, line 8 to p 4, line 4].
Regarding instant claim 12 (dependent from instant claim 1), as Boisart discloses degrading the plastic products such as polyethylene to monomers [abstract, p 3 lines 8-12], the method is considered to produce the monomer of an alkane.
Regarding instant claim 14 (dependent from instant claim 1), as the enzyme of UNI1 is encompassed by the structural limitations of the enzyme in the claims, it is considered to have the increased ability to degrade polyolefin compared to a corresponding genetically unmodified enzyme or fragment thereof, as the function of the enzyme is considered inherent to its structure (MPEP 2112.I).
Regarding instant claim 15 (dependent from instant claim 1), the enzyme of UNI1 does not disclose a signal sequence, and is therefore considered to not comprise a signal sequence and therefore is considered not to be secreted out of the cell which produces it.
Regarding instant claim 16 (dependent from instant claim 1), the limitation “wherein the enzyme or fragment thereof is encoded by a heterologous nucleotide sequence” does not structurally limit the enzyme used in the method of instant claim 1. Additionally, the phrase “heterologous nucleotide sequence” is considered a product-by-process limitation, as the origin of the nucleotide being heterologous and therefore the production of the nucleotide sequence does not impose any structural limitations on the product of the nucleotide sequence itself (MPEP 2113.I). As UNI1 discloses a chloroperoxidase from the naturally occurring Bacillus cereus, it is considered to be encoded by a nucleotide sequence.
Regarding instant claims 2 and 6 (dependent from instant claim 2), UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
Regarding instant claim 9 (dependent from instant claim 2), the enzyme of UNI1 is considered have the capability of degrading the polyolefin in the presence or absence of hydrogen peroxide at a temperature of at least 20 °C, at least 25 °C, at least 30 °C, at least 37 °C or at a temperature of 30 – 95 °C, as the enzyme of UNI1 satisfies the structural limitations of the claims, and the function of the enzyme is presumed to be inherent to its structure (MPEP 2112.I).
Regarding instant claim 11 (dependent from instant claim 9), the enzyme of UNI1 is considered have the capability of degrading the polyolefin in the presence of hydrogen peroxide and the hydrogen peroxide, as the enzyme of UNI1 satisfies the structural limitations of the claims, and the function of the enzyme is presumed to be inherent to its structure (MPEP 2112.I). The limitations of instant claim 11 regarding the production of hydrogen peroxide by another in lines 4-6 do not structurally limit the enzyme of instant claim 11.
Regarding instant claim 18 (dependent from instant claim 2), as UNI1 discloses a chloroperoxidase from the naturally occurring Bacillus cereus, it is considered to be encoded by a polynucleotide.
Regarding instant claims 19 (dependent from instant claim 18) and 21 (dependent from instant claim 2), Boisart discloses the method of enzymatic polyolefin degradation as discussed in the rejection of claim 1 above comprising cloning a gene of interest for into a vector [p 19, lines 10-12] for expression of the encoded enzyme in the host cell E. coli [p 19, lines 1-2], and UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus.
Regarding instant claim 23 (dependent from instant claim 2), UNI1 discloses the non-heme chloroperoxidase from Bacillus cereus.
Regarding instant claim 3, Boisart discloses the method of enzymatic polyolefin degradation as discussed in the rejection of instant claim 1 above comprising cloning a gene of interest for into a vector [p 19, lines 10-12] for expression of the encoded enzyme in the host cell E. coli [p 19, lines 1-2], wherein the method can be carried out with enzymes that include peroxidase [p 4, lines 9-14], and UNI1 discloses a non-heme chloroperoxidase from Bacillus cereus that shares 97.2% identity with SEQ ID NO: 2 and has Ser97, Asp221, His249, Gly99, Pro126 and Gly218 of SEQ ID NO: 2 [see Appendix B]. As the enzyme of UNI1 satisfies the structural limitations of the claim, it is considered to have the function of being capable of degrading polyolefins, as the function is considered inherent to the structure of the enzyme (MPEP 2112.I).
It would have been obvious before the effective filing date for one of ordinary skill in the art to modify the combined method of the reference application, Boisart and UNI1 by incorporating the polynucleotide encoding the enzyme of UNI1 into a vector for expression in a host cell, as taught by Boisart, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined method of the reference application, Boisart and UNI1 by incorporating the polynucleotide encoding the enzyme of UNI1 into a vector for expression because Boisart discloses the cloning and expression of enzymes capable of degrading polyolefins such as peroxidases to carry out the method of degrading polyolefins, and UNI1 discloses a peroxidase. One of ordinary skill in the art would have had a reasonable expectation of success because Boisart and UNI1 relate to peroxidases.
Regarding instant claim 10 (dependent from instant claim 3), the combined method of the reference application, Boisart and UNI1 comprises a host cell which is considered to have the activity of being capable of degrading the polyolefin in the presence or absence of hydrogen peroxide at a temperature of at least 20 °C, at least 25 °C, at least 30 °C, at least 37 °C or at a temperature of 30 – 95 °C, as the host cell from the combined method satisfies the structural limitations of the instant claims, and the function of the cell is presumed to be inherent to its structure (MPEP 2112.I).
Regarding instant claim 17 (dependent from instant claim 3), Boisart discloses the host cell is E. coli [p 19, lines 1-2].
Regarding instant claim 22 (dependent from instant claim 3), the enzyme of UNI1 shares 97.2% sequence identity with SEQ ID NO: 2 and is from Bacillus cereus [see Appendix B].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Remarks: beginning on page 23 of Applicant’s response to double patenting rejections; Applicant in summary requests rejections be held in abeyance until the remaining rejections are overcome.
Applicant’s request is acknowledged and the rejections are updated to the instant claim amendments.
EXAMINER COMMENT
The polypeptides comprising the amino acid sequence of SEQ ID NOs: 2, 4, 6, and 8 are free of the prior art.
Conclusion
Status of the Application:
Claims 1-3, 5-12, 14-19 and 21-23 are pending.
Claims 1-3, 5-12, 14-19 and 21-23 are rejected.
No claim is in condition for allowance.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JOSEPH SPANGLER whose telephone number is (571)270-0314. The examiner can normally be reached M-F 7:30 am - 4:30 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath Rao can be reached at (571) 272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/JOSEPH R SPANGLER/
Examiner
Art Unit 1656
/David Steadman/Primary Examiner, Art Unit 1656
APPENDIX A
PNG
media_image1.png
427
651
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Greyscale
Sequence alignment of SEQ ID NO: 2 with NCBI Accession No. WP_04290493.1, where * denotes the locations of Ser97, Asp221, His249 of SEQ ID NO: 2, and + denotes the locations of Gly99, Pro126, and Gly218 of SEQ ID NO: 2.
APPENDIX B
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media_image2.png
494
633
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Greyscale
Sequence alignment of SEQ ID NO: 2 with UniProt Accession No. A0A161QNJ7_BACCE, where * denotes the locations of Ser97, Asp221, His249 of SEQ ID NO: 2, and + denotes the locations of Gly99, Pro126, and Gly218 of SEQ ID NO: 2.
Prosecution Insights