DETAILED ACTION
Applicant’s amendment submitted 5/18/2026 is acknowledged. Claims 1, 29-30, 39, 42, and 49 are currently amended. Claims 1-79 are pending in the instant application.
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-56 and 58-64, and the species: D102Q, G125S, T137A, S153N, N154H, F221L, T227K, F249L, V266L, and N300Y (claim 7 (i) – corresponds to SEQ ID NO: 10) and Burkholderia cepacia in the reply filed on 5/18/2026 is acknowledged. Claims 57 and 65-79 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 5/18/2026.
The species election for the cells for codon optimization of nucleic acid sequence encoding the recombinant mutant lipase and the host cell are hereby withdrawn by the Examiner and all species rejoined.
Priority
The instant application is a U.S. National Phase of PCT/US2022/077426, filed 9/30/2022, and claims Domestic Benefit to U.S. Provisional Application No. 63/250,403, filed 9/30/2021.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 5/18/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Objections
Claims 8, 29, 32, 47, and 59 are objected to because of the following informalities:
Claims 8, 29, and 32 are missing commas after the recitation of the preambles.
Appropriate correction is required.
Claim 47 ungrammatically recites “wherein the lipase digests greater than 50%, 60%...of ingested fats in the small intestine of a subject to fatty acids and monoglycerides” but should instead recite “wherein the lipase digests greater than 50%, 60%...of ingested fats to fatty acids and monoglycerides in the small intestine of a subject.”
Claim 59 comprises an unnecessary comma after the recitation of “protease” in line 2.
Claims 5-56 and 58-64 are objected to under 37 CFR 1.75(c) as being in improper form because a multiple dependent claim cannot depend from any other multiple dependent claim. See MPEP § 608.01(n). The claims are objected to because they may depend from a claim that is multiple dependent. In the interest of compact prosecution and examination of these claims on the merits, see the claim interpretations below.
Claim Interpretation
Claim 1 is drawn to a recombinant mutant microbial lipase enzyme, wherein the lipase comprises one or more of (i) increased stability at acidic pH relative to a corresponding wild-type microbial lipase enzyme, (ii) increased stability in the presence of a protease relative to the corresponding wild-type microbial lipase enzyme, or (iii) at least 60%, 70%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% of the enzymatic activity of the corresponding wild-type microbial lipase enzyme.
Under the broadest reasonable interpretation, claim 1 includes any microbial lipase that contains any modified sequence wherein the microbial lipase comprises one or more of (i) increased stability at acidic pH relative to its corresponding wild-type lipase, (ii) increased stability in the presence of a protease relative to the corresponding wild-type microbial lipase, or (iii) at least 60%, 70%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% of the enzymatic activity of the corresponding wild-type microbial lipase. The microbial lipase can be obtained by any sequence modification techniques, as recombination is only an intended preamble limitation and equivalent lipases can be achieved by the sequence modification techniques other than recombination.
Claim 1 receives adequate written description support and is not rejected under 35 U.S.C. 112(a) for the following reasons:
Applicant depicts in Figure 4 a sequence alignment demonstrating the conservation of amino acids among the lipase sequences of Pseudomonas aeruginosa PAO1 from family I.1 and comprising SEQ ID NO: 29, Pseudomonas fluorescens from family I.1 and comprising SEQ ID NO: 30, Burkholderia cepacia from family I.1 and comprising SEQ ID NO: 1, Burkholderia glumae from family I.2 and comprising SEQ ID NO: 31, Chromobacterium viscosum from family I.2 and comprising SEQ ID NO: 32, Pseudomonas luteola from family I.2 and comprising SEQ ID NO: 33, Pseudomonas fluorescens ABA72135 from family I.1 and comprising SEQ ID NO: 34, Pseudomonas fluorescens AEV60646 from family I.1 and comprising SEQ ID NO: 35, Pseudomonas sp WP-015093259 from family I.3 and comprising SEQ ID NO: 36, Pseudomonas fragi CAA32193 from family I.1 and comprising SEQ ID NO:37, Pseudomonas fragi CAC07191 from family I.1 and comprising SEQ ID NO: 38, Pseudomonas stutzeri comprising SEQ ID NO: 41, and Pseudomonas mendocina LipA comprising SEQ ID NO: 42. Applicant has indicated the catalytic triad active site and calcium binding site across all 13 microbial lipases. Sites selected for amino acid substitutions are also depicted in Figure 4. Applicant further depicts in Figure 5 a sequence alignment demonstrating the conservation of residues between Burkholderia cepacia from family I.1 and comprising SEQ ID NO: 1, Burkholderia glumae from family I.2 and comprising SEQ ID NO: 31, Chromobacterium viscosum from family I.2 and comprising SEQ ID NO: 32, and Pseudomonas luteola from family I.2 and comprising SEQ ID NO: 40. Applicant has indicated the conserved amino acids that constitute the oxyanion hole, the lid, the subdomain, the catalytic triad, and calcium binding site. Figure 5 also depicts the sites selected for amino acid substitution. Figure 2 depicts a ribbon model of a lipase from Burkholderia cepacia with amino acids 118-159 defining the lid, amino acid 214-261 defining the subdomain that faces the lid, residues 262-320 including alpha helix 11 and amino acid 160-213 including alpha helix 7. Additionally, the catalytic triad residues – serine 87, aspartic acid 264, and histidine 286 – are illustrated in Figure 2. Figure 6 depicts a three-dimensional model of B. cepacia lipase showing the locations of the catalytic lid, the oxyanion hole, the catalytic triad, the calcium domains, and the positions of the variant substitutions. In Figures 13-20B, 22-27, and 29-31B, several mutants lipases are disclosed with testing for stability at acidic pH, half-life testing, testing for stability of the mutant lipases in the presence of a protease, testing of the mutant lipases activity at acidic pH, and activity after administration in animals.
Applicant has set forth the conserved sequences and functional domains across 13 lipase species spanning the families I.1-I.3 in several representative microbial lipase species and the residues targeted for substitution that impart the functional limitations required in claim 1. Accordingly, Applicant has demonstrated an adequate written description for the broad genus claimed in claim 1.
Claims 4, 6, 8-10, 12-14, 18, 21-22, 24-25, 27-30, 32-51, and 58 are interpreted to depend from claim 1.
Claim 7 is interpreted to depend from claim 5.
Claim 26 is interpreted to depend from claim 24.
Claim 31 is interpreted to depend from claim 29.
Claim 55 is interpreted to depend from claim 52.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 23, 38, and 42 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 23 recites “a recombinant mutant microbial lipase enzyme comprising a substitution, or combination of substitutions, listed in Table 1 or Table 2.” Claim 23 is indefinite for referencing to tables. See MPEP 2173.05(s). The substitutions indicated in Tables 1 and 2 are to be recited in the claim to clearly indicate the substitution limitations required in the claim. Furthermore, Table 1 lists “Exemplary Substitutions – Embodiments 1 and 2” and, thus it is not clear if the listed substitutions are only exemplary or are exhaustive. Therefore, the metes and bounds of claim 23 cannot be determined, and claim 23 is indefinite.
Regarding claim 38, the term "preferentially" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d). It is not clear if the lipase of claim 38 must hydrolyze the sn-1 and sn-3 positions on a triglyceride or if these positions are only preferred embodiments and not necessary. Thus, the metes and bounds of claim 38 are unclear.
The term “sufficiently active” in claim 42 is a relative term which renders the claim indefinite. The term “sufficiently active” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. It is not clear what degree of activity would be considered sufficient as required by claim 42. The specification at paragraphs [0030] and [0158] exemplify degrees in which the recombinant mutant lipase is more active than a pancrelipase when tested under the same condition and is further recited in claim 43; however, this is not recited in claim 42. Therefore, one of ordinary skill in the art would not be able to determine the metes and bounds of the claimed limitation.
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.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], 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 5-10, 12-14, 18, 21-22, 24-42, 44-51, 58, and 61-64 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, 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.
Claims 6-10, 12-14, 18, 21-22, 24-42, 44-51, 58, and 61-64 are improper multiple dependent claims since they depend from at least one other multiple dependent claim. Consequently, the limitations required by each claim are ambiguous.
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 § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 6, and 8-56 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Yoshida (WO2018/0021324; citations corresponding to PE2E English translation provided) as evidenced by Kim et al. (Structure, 1997, Vol. 5(2), pp.173-185; of record in IDS filed 5/18/2026) and UniProt – Burkholderia cepacia Triacylglycerol lipase; herein after UniProt (retrieved from lip - Triacylglycerol lipase - Burkholderia cepacia (Pseudomonas cepacia) | UniProtKB).
Regarding claim 1, Yoshida teaches polypeptides having lipase activity derived from Burkholderia cepacia with improved stability in acidic pH (see Abstract, p.27, 4th passage-p.28, 4th passage, Table 13, and Fig. 8).
Regarding claim 6, Yoshida teaches the polypeptide having lipase activity derived from Burkholderia cepacia with improved stability in acidic pH has three mutations – P233G/L234E/V235M – compared to the wild-type, reading on three mutations relative to the corresponding wild-type microbial lipase (see p.27, 4th passage-p.28, 4th passage, Table 13, and Fig. 8).
Regarding claim 8, Yoshida teaches the lipase is derived from Burkholderia cepacia and comprises multiple α-helices and β-sheets (see Abstract, p.3, 3rd passage,-p.4,4th passage, and Figs.1-7). Kim provides evidence that the lipase from Pseudomonas cepacia is an α/β-hydrolase lipase (see Abstract – Results, p.174, left column, last passage, p.176, 1st passage,-last passage, and p.182, passage bridging left and right columns). UniProt provides evidence that Burkholderia cepacia is also known as Pseudomonas cepacia (see p.1 -- Organism). Thus, the lipase of Yoshida is an α/β-hydrolase lipase.
Regarding claim 9, the sequence alignment of the lipase of Yoshida comprising SEQ ID NO: 5 comprises the catalytic triad of Ser87, Asp264, and His286 (see Appendix A for sequence alignment).
Regarding claim 10, Kim provides evidence that the lipase of Pseudomonas cepacia (Burkholderia cepacia) comprises a hydrophobic lid that allows for binding and lipolysis (see Abstract – Results and Conclusions, p.174, right column, 2nd passage, p.177, left column, 1st passage, p.180, right column and last passage, 1st passage, p.181, left column, 1st and 2nd passages, p.182, right column, 2nd passage, and Fig. 9). Thus, the lipase of Yoshida comprising SEQ ID NO: 5 is expected to comprise the hydrophobic lid that allows for binding and lipolysis.
Regarding claim 11, Kim provides evidence that Pseudomonas cepacia (Burkholderia cepacia) lipase hydrolyzes triglycerides with a chain length greater than or equal to eight (see p.174, right column, last passage). Yoshida further confirms the lipase of their disclosure retains activity toward triglycerides (see p.22, 5th passage).
Regarding claim 12, Kim provides evidence that Pseudomonas cepacia (Burkholderia cepacia) lipase comprises a calcium binding site that stabilizes the lipase when calcium is bound (see Abstract – Results, p.178, last passage,-p.179, right column, 1st passage, and Table 1). Kim discloses the calcium binding site comprises Asp242, Asp288, Gln292, and Val296, which are present in the lipase of Yoshida (see Appendix A for sequence alignment).
Regarding claim 13, Kim provides evidence that Pseudomonas cepacia (Burkholderia cepacia) lipase comprises an oxyanion hole that stabilizes a negatively charged intermediate generated during fatty acid bond hydrolysis (see Abstract – Conclusions, p.179, right column, last passage,-p.180, left column, 1st passage, p.182, left column, 2nd passage, right column, 2nd passage, and Figs. 6-7). Kim discloses the oxyanion hole is comprised of Leu17 and Gln88, which are present in the lipase of Yoshida (see Appendix A for sequence alignment).
Regarding claims 14-20, the instant specification at paragraph [0055] provides evidence that lipase from Burkholderia cepacia is a family I.2 lipase. Thus, the lipase of Yoshida is considered to read on claims 14-20.
Regarding claim 21, Yoshida teaches the lipase comprising SEQ ID NO: 5 comprises Ser87, Asp264, and His286 (see Appendix A for sequence alignment).
Regarding claim 22, Yoshida discloses a lipase comprising SEQ ID NO: 5 that has 96.9% sequence identity to SEQ ID NO: 10 of the instant invention and thus has at least 96% sequence identity to SEQ ID NO: 10 of the instant invention (see Appendix A for sequence alignment).
Regarding claim 23, the lipase of Yoshida comprising SEQ ID NO: 5 comprises I12, V26, Q34, T79, V84, T92, V126, L134, T137, V138, I139, V143, I148, L161, V220, T224, T227, I232, L234, V235, V266, S281, L287, and V305 as set forth in Table 1 (see Appendix A for sequence alignment).
Regarding claims 24-37, the lipase of Yoshida comprises all structural limitations required and is expected to comprise all functional features of claims 24-37, absent evidence to the contrary.
Regarding claim 38, in view of the lack of clarity of the claim as set forth above in the 35 U.S.C. 112(b) rejection, any hydrolysis of triglycerides is considered to read on the claim. Yoshida teaches the lipase of their disclosure hydrolyzes triglycerides (see p.22, 5th passage). Further, the specification at paragraph [0239] provides that B. cepacia lipase catalyzes the hydrolysis of triglycerides to produce fatty acids and monoglycerides with greater level of activity against the sn-1 and sn-3 regions of the triglyceride. Thus, the B. cepacia lipase of Yoshida is considered to read on claim 38.
Regarding claim 39, the specification at paragraph [0239] provides evidence that B. cepacia lipase is stable in the presence of bile salts. Therefore, the B. cepacia lipase of Yoshida is considered to also be stable in presence of bile salts.
Regarding claim 40, the specification at paragraph [0239] provides evidence that B. cepacia lipase does not require a co-lipase for catalytic activity. Therefore, the B. cepacia lipase of Yoshida is considered to not require a co-lipase.
Regarding claim 41, Yoshida does not teach their lipase is cross-linked or crystallized and thus reads on the claim.
Regarding claim 42, in view of the lack of clarity of the limitation of “sufficiently active,” any retention of activity at acidic pH is considered to read on the claim. Yoshida teaches improved activity of their lipase at acidic pH (p.27, 4th passage-p.28, 4th passage, Table 13, and Fig. 8).
Regarding claims 43-50, the B. cepacia lipase of Yoshida comprising SEQ ID NO: 5 comprises all structural limitations of the claimed invention and is expected to impart the functional features are required by claims 43-50.
Regarding claim 51, Yoshida teaches nucleic acids encoding lipases of their invention (see p.19, 4th passage).
Regarding claim 52, Yoshida teaches recombinant expression vectors that encode the nucleic acids encoding the lipases of their invention (p.19, 6th passage).
Regarding claim 53, Yoshida teaches the recombinant expression vectors are optimized for expression in the heterologous host cell (see p.19, 6th passage,-p.20, 1st passage).
Regarding claim 54, Yoshida teaches the expression vector can be optimized for expression in E. coli (see p.19, 6th passage,-p.20, 1st passage).
Regarding claims 55-56, Yoshida teaches an E. coli host cell comprising an expression vector encoding a B. cepacia lipase comprising SEQ ID NO: 5 (see p.23, 3rd passage,-28, 4th passage).
Claims 1-6, 9-10, 18, and 22-37 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt – A0ABR5T3C6_9BURK (published 2015; hereinafter 9Burk; retrieved from Alpha/beta hydrolase - Burkholderia savannae | UniProtKB).
Regarding claims 1-6, 10, 18, 22, and 23, 9Burk discloses an alpha/beta hydrolase lipase from Burkholderia savannae that comprises 27 amino acid substitutions and the specific substitutions D102Q, S153N, F221L, F249L, V266L, and N300Y as compared to wildtype B. cepacia and has 93.2% sequence identity to SEQ ID NO: 10 of the instant invention (see Appendix C for sequence alignment).
Regarding claims 9 and 21, the alpha/beta hydrolase lipase of 9Burk comprises Ser87, Asp264, and His286 and thus comprises the catalytic triad (see Appendix C for sequence alignment).
Regarding claims 24-37, the 9Burk lipase comprises all structural limitations required and is expected to comprise all functional features of claims 24-37, absent evidence to the contrary.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 58-64 are rejected under 35 U.S.C. 103 as being unpatentable over Yoshida (WO2018/0021324; citations corresponding to PE2E English translation provided) as evidenced by Kim et al. (Structure, 1997, Vol. 5(2), pp.173-185; of record in IDS filed 5/18/2026) and UniProt – Burkholderia cepacia Triacylglycerol lipase; herein after UniProt (retrieved from lip - Triacylglycerol lipase - Burkholderia cepacia (Pseudomonas cepacia) | UniProtKB), as applied to claims 1, 6, and 8-56 above, and further in view of Shlieout et al. (WO2005/092370).
Yoshida as evidenced by Kim and UniProt teach the invention of claim 1 as outlined in the rejection above.
Regarding claims 58 and 61, Yoshida teaches compositions comprising polypeptides encoding lipases of their invention such as that comprising SEQ ID NO: 5 (see p.31, 8th passage).
Yoshida does not teach a pharmaceutical composition comprising a pharmaceutically acceptable carrier and/or an excipient or that the composition is an oral composition.
Shlieout teaches oral pharmaceutical compositions of lipase-containing products for oral administration wherein the lipase is of microbial origin and wherein the pharmaceutical composition provides improved lipolytic activity and stabilization of the lipase in acidic pH range that are formulated for maldigestion characterized by deficiency in lipase, protease, and/or amylase (see Abstract and p.1, 1st-2nd paragraph). The oral pharmaceutical compositions further comprise carriers and excipients, reading on claims 58 and 61 (see p.19, 2nd paragraph, p.22, 1st-2nd paragraphs, and p.43, 2nd passage).
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have added a carrier and excipient, as taught by Shlieout, to the composition comprising polypeptides encoding a lipase comprising SEQ ID NO: 5, as taught by Yoshida, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to provide the composition in an oral pharmaceutical for maldigestion to provide further stability at acidic pH range, yielding predictable results. There would have been a reasonable expectation of success because Yoshida and Shlieout are directed to lipase compositions.
Regarding claims 59 and 60, Yoshida does not teach the pharmaceutical composition further comprises a microbial protease and/or a microbial amylase.
Shlieout further teaches the pharmaceutical composition comprises a microbial protease and amylase, most preferably Aspergillus melleus protease and Aspergillus oryzae amylase (see paragraph bridging pp.15-16, p.16, 2nd-3rd paragraphs, p.17,4th and last paragraph, p.46, 2nd passage).
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have further included Aspergillus melleus protease and Aspergillus oryzae amylase, as taught by Shlieout, to the oral pharmaceutical composition comprising a lipase comprising SEQ ID NO: 5, a carrier, and excipient, as taught by Yoshida in view of Shlieout, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to formulate the oral pharmaceutical composition for maldigestion characterized by deficiency in lipase, protease, and amylase, yielding predictable results.
Regarding claims 62 and 63, Yoshida does not teach the pharmaceutical composition is formulated as a powder, granulate, pellet, micropellet, liquid, a tablet, encapsulated in a capsule, or formulated as a tablet dosage form.
Shlieout teaches the pharmaceutical composition comprising a lipase is formulated as a powder, pellet, granule, tablet, or microspheres filled into capsules, reading on encapsulated in capsule as recited in claim 63 (see p.25, 3rd paragraph, p.45, 3rd passage).
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have formulated the oral pharmaceutical composition comprising a lipase comprising SEQ ID NO: 5, a carrier, and excipient, as taught by Yoshida in view of Shlieout, as a powder, pellet, granule, tablet, or microspheres filled into capsules, as taught by Shlieout, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to provide the oral pharmaceutical composition in accepted formulations for oral administration, yielding predictable results.
Regarding claim 64, the oral pharmaceutical composition comprising a lipase comprising SEQ ID NO: 5, a carrier, and excipient as taught by Yoshida in view of Shlieout, does not comprise an enteric coating. Further, Shlieout teaches the pharmaceutical composition does not comprise an enteric coating (see p.4, 1st-2nd paragraphs).
Thus, claims 58-64 are prima facie obvious over Yoshida in view of Shlieout.
Closest Prior Art
Claims 3 and 7 are free of the prior art. SEQ ID NOs: 2-14 are free of the prior art. The closest prior art is to Yoshida (WO2018/0021324). Yoshida discloses a lipase comprising SEQ ID NO: 5 and that has 96.9% sequence identity to SEQ ID NO: 10 (corresponds to element i) in claim 7) of the instant invention (see Appendix A for sequence alignment). SEQ ID NO: 5 of Yoshida has 99% sequence identity to SEQ ID NO: 2 (corresponds to element a) in claim 7) of the instant invention (see Appendix B for sequence alignment). However, SEQ ID NO: 5 of Yoshida does not comprise any of the positional mutations and specific mutations as recited in claims 3 and 7.
Conclusion
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/J.P.S./Examiner, Art Unit 1651
/MELENIE L GORDON/Supervisory Patent Examiner, Art Unit 1651
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