DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of the Application
Receipt of the Response and Amendment after Non-Final Office Action filed 12/30/2025 is acknowledged.
Applicant has overcome the following rejections by virtue of the amendment: the 35 U.S.C. §112(b) rejections of claims 7 and 14 have been withdrawn.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 1, 7-9, 14, 21, 26-27, 88-89, 91-95, 97, 107-108, 111, 116
Withdrawn claims: 26-27, 88-89, 91-95, 97, 107-108, 111, 116
Previously cancelled claims: 2-6, 10-13, 15-20, 22-25, 28-87, 90, 96, 98-106, 109-110, 112-115, 117-314
Newly cancelled claims: None
Amended claims: 1, 7, 14
New claims: None
Claims currently under consideration: 1, 7-9, 14, 21
Currently rejected claims: 1, 7-9, 14, 21
Allowed claims: None
Claim Rejections - 35 USC § 103
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 1, 7, 9, 14, and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Jimenez-Flores (US 2021/0045398; previously cited), hereinafter referred to as “Jimenez”, in view of Beliciu (Beliciu, C.M., Moraru, C.I., “Physico-chemical changes in heat treated micellar casein – Soy protein mixtures”, 2013, LWT – Food Science and Technology, vol. 54, pages 469-476; previously cited) as evidenced by Sadiq (Sadiq et al., “Casein Micelles as an Emerging Delivery System for Bioactive Food Components”, 2021, Foods, vol., 10, 1965; previously cited).
Regarding claims 1 and 7, Jimenez teaches a stable structure (corresponding to a “stable blend of casein and plant protein”) formed by swelling casein micelles through removal of calcium from the casein micelles; incorporating globular proteins into the swelled micelle; and adding calcium into the swelled micelle so that the micelle is no longer swollen but contains the incorporated globular proteins in the interior of the micelle ([0005], Fig. 1). Jimenez teaches that the casein micelle is a traditional casein micelle [0026]; therefore, the structure made from the casein micelle comprises: an outer layer comprising κ-casein; and an interior comprising a casein protein comprising αs1-casein, αs2-casein, and β-casein, as evidenced by Sadiq (page 3, paragraph 4; page 4, Table 1). Jimenez teaches that the globular protein inside the structure ([0005], Fig. 1) may be soybean protein [0027], [0033]. Jimenez also discloses that the casein micelles are incorporated into foods such as yogurt, cheese, and pudding [0043], which require gelling abilities.
Jimenez does not teach that the soybean protein is soybean glycinin as recited in present claim 1; or that the interior of the casein micelle further comprises soy globulin 7S and 11S as recited in present claim 7.
However, Beliciu teaches that soybean protein contains four protein fractions including fractions containing glycinin and soybean globulin 7S and 11S (page 469, 2nd column, 2nd paragraph- page 470, 1st column, 1st paragraph). Beliciu teaches both casein and soy proteins have many uses in the food industry and that there is an interest in using mixtures of these proteins (page 469, 1st column, 1st paragraph). Beliciu also teaches that glycinin is combined with casein micelles (page 470, 1st column, 2nd paragraph; page 475, 2nd column, 3rd paragraph). Beliciu also discloses that the ratio of 7S and 11S (corresponding to ratio of glycinin:β-conglycinin) greatly affects the gel properties of the protein solutions (page 470, 1st column, 1st paragraph)
It would have been obvious for a person of ordinary skill in the art to have modified the structure of Jimenez to include soy glycinin and soy globulin 7S and 11S as taught by Beliciu. Since Jimenez teaches that its structure comprises casein micelles and soy protein ([0005], [0033], Fig. 1); and that the casein micelles are incorporated into foods such as yogurt, cheese, and pudding [0043], which require gelling abilities, but Jimenez does not disclose a type of soy protein to mix with casein micelles that may be used in foods requiring gelling abilities, a skilled practitioner would have been motivated to consult an additional reference such as Beliciu to determine suitable soy proteins to combine with casein micelles. A skilled practitioner would have been motivated to select glycinin and soy globulin 7S and 11S from the four types of soybean protein disclosed in Beliciu because this list of Beliciu provides a finite number of identified, predictable solutions (i.e., types of soybean protein which may be combined with casein micelles) with a reasonable expectation of success. MPEP §2143.I.E. It is also noted that a skilled practitioner may use non-fractionated soy protein as the soy protein of Jimenez so as to increase nutritional value (Beliciu, page 469, 1st column, 1st paragraph). In this case, the casein micelle of Jimenez would include all four fractions of soy protein including glycinin and soy globulin 7S and 11S. For these reasons, the claimed soybean glycinin recited in present claim 1 and the claimed soy globulins 7S and 11S recited in present claim 7 are rendered obvious.
Regarding claim 9, Jimenez teaches the invention as described above in claim 1, including the structure is formed by swelling casein micelles through removal of calcium from the casein micelles; incorporating globular proteins into the swelled micelle; and adding calcium into the swelled micelle so that the micelle is no longer swollen but contains the incorporated globular proteins ([0005], Fig. 1). Jimenez teaches that the casein micelle is a traditional casein micelle [0026]; therefore, the structure made from the casein micelle comprises an interior comprising αs1-casein, αs2-casein, and β-casein, as evidenced by Sadiq (page 3, paragraph 4; page 4, Table 1).
Regarding claim 14, Jimenez teaches the invention as described above in claim 1, including the structure is incorporated into a dairy composition (corresponding to dairy product) [0043]. Jimenez also teaches that the structure confers upon the dairy composition characteristics selected from the group consisting of: appearance (corresponding to an appearance of skim milk) (Figure 7B; [0015]) and structure (corresponding to casein micelles existing as a colloidal suspension in milk [0004] and the structure formed by the combination of casein micelle and globular protein forming a stable colloidal suspension [0031]).
Regarding claim 21, modified Jimenez teaches the invention as described above in claim 1, including the structure is formed by providing a solution comprising soybean glycinin (Beliciu, page 469, 2nd column, 2nd paragraph); and mixing at least two casein proteins (corresponding to the κ-casein, αs1-casein, αs2-casein, and β-casein in the distended casein micelle) in the solution comprising the soybean glycinin (Jimenez, Figure 1, [0005]).
Claims 1 and 8 are rejected under 35 U.S.C. 103 as being unpatentable over Wolff (WO 2022/038601; previously cited) in view of Beliciu (Beliciu, C.M., Moraru, C.I., “Physico-chemical changes in heat treated micellar casein – Soy protein mixtures”, 2013, LWT – Food Science and Technology, vol. 54, pages 469-476; previously cited) as evidenced by Sadiq (Sadiq et al., “Casein Micelles as an Emerging Delivery System for Bioactive Food Components”, 2021, Foods, vol., 10, 1965; previously cited).
Regarding claim 1, Wolff teaches a stable structure (corresponding to casein micelles) comprising κ-casein, αs1-casein, and αs2-casein (page 3, lines 5-6, 8; page 4, lines 22-23). Since αs1-casein and αs2-casein are located in the interior of a casein micelle and κ-casein is located on the exterior of a casein micelle as evidenced by Sadiq (page 3, paragraph 4; page 4, Table 1), Wolff teaches that the structure comprises: an outer layer comprising κ-casein; and an interior comprising αs1-casein and αs2-casein as claimed. Wolff also discloses that a non-milk particle comprising soy protein or a fraction thereof is part of the micelle (page 15, lines 13-15, 22-25). Wolff does not specify that the soy protein is located in the interior of the micelle; however, since being a part of the micelle only presents two options (i.e., an outer layer of the micelle; or an interior of the micelle), a skilled practitioner would “at once envisage” the soy protein being located in the interior of the micelle and thus, “at once envisage” the claimed arrangement to meet the claimed structure, especially wherein encapsulating molecules within the interior of a casein micelle is known in the art and wherein these two options (i.e., inside or outside of the micelle) provide a finite number of identified, predictable solutions with a reasonable expectation of success. MPEP §2143.I.E.
Wolff does not teach that the soybean protein is soybean glycinin.
However, Beliciu teaches that soybean protein contains four protein fractions including a fraction consisting of the soy globulin glycinin (page 469, 2nd column, 2nd paragraph). Beliciu teaches both casein and soy proteins have many uses in the food industry and that there is an interest in using mixtures of the proteins (page 469, 1st column, 1st paragraph). Beliciu also teaches that glycinin is combined with casein micelles (page 470, 1st column, 2nd paragraph; page 475, 2nd column, 3rd paragraph).
It would have been obvious for a person of ordinary skill in the art to have modified the structure of Wolff to include soy glycinin as taught by Beliciu. Since Wolff teaches that its structure comprises casein micelles and soy protein or a fraction thereof (page 15, lines 13-15, 22-25), but does not disclose a type of soy protein or a fraction thereof, a skilled practitioner would have been motivated to consult an additional reference such as Beliciu to determine a suitable soy protein or a fraction thereof to combine with casein micelles. A skilled practitioner would have been motivated to select glycinin from the four types of soybean protein disclosed in Beliciu because this list of Beliciu provides a finite number of identified, predictable solutions (i.e., types of soybean protein which may be combined with casein micelles) with a reasonable expectation of success. MPEP §2143.I.E. It is also noted that a skilled practitioner may use non-fractionated soy protein as the soy protein of Wolff so as to increase nutritional value (Beliciu, page 469, 1st column, 1st paragraph). In this case, the casein micelle of Wolff would include all four fractions of soy protein including glycinin. For these reasons, the claimed soybean glycinin is rendered obvious.
Regarding claim 8, Wolff teaches the invention as described above in claim 1, including the structure does not comprise β-casein (page 3, lines 5-6, 8).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1 and 7-9 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 86-90, 95-98, and 100-105 of co-pending Application No. 18/855,187 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because instant claims 1, 8, and 9 require a structure comprising an outer layer of κ-casein; and an interior comprising at least one soybean glycinin and at least one of αs1-casein, αs2-casein, and β-casein. Co-pending claims 86, 100, 101, 102, 103, 104, and 105 also require a casein micelle comprising an outer layer of κ-casein; and an interior comprising soybean glycinin and at least one of αs1-casein, αs2-casein, and β-casein. Instant claim 1 also requires that the structure is stable whereas the co-pending claims do not require the structure to be stable. However, a micelle comprising an outer layer and an interior layer as recited in the co-pending claims at least suggests that the micelle is stable enough for at least some amount of time to provide this specific structure. Therefore, the structure of the co-pending claims is considered to be stable, especially wherein the instant claims does not require the structure to be stable for any specific amount of time. As such, instant claims 1, 8, and 9 are rendered obvious by co-pending claims 86, 100, 101, 102, 103, 104, and 105.
Instant claim 7 further requires that the interior of the structure further comprises soy globulin 7S (also known as β-conglycinin in the field of the art) and 11S (also known as glycinin in the field of the art) wherein the ratio of 7S and 11S (7S/11S) is lower than a naturally-occurring ratio. Co-pending claims 87-90 and 95-98 also requires that the structure comprises 7S and 11S in a ratio of 7S/11S that is lower than a naturally-occurring ratio. Therefore, instant claim 7 is rendered obvious by co-pending claims 87-90 and 95-98.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
Claim Rejections – 35 U.S.C. §112(b) of claims 7 and 14: Applicant amended claims 7 and 14 to fully address the rejections; therefore, the rejections are withdrawn.
Claim Rejections – 35 U.S.C. §103 of claims 1, 9, 14, and 21 over Jimenez and Beliciu as evidenced by Sadiq; claims 1 and 8 over Wolff and Beliciu as evidenced by Sadiq; claim 7 over Jimenez and Beliciu as evidenced by Sadiq and Yang: Applicant’s arguments have been fully considered and are considered unpersuasive.
Applicant argued that evidence within Jimenez confirms that the plant proteins and casein micelles within its “stable blend”, “stable suspension”, or “co-dispersion” remain distinct. Applicant pointed to Table 2 and Fig. 6 of Jimenez as showing that the increase in casein micelle size is consistent with swelling of the micelle, not with internal incorporation of a secondary protein into the core of the micelle. Applicant pointed to Fig. 1 of Jimenez as showing that the plant proteins are separate entities positioned near “Distended Casein Micelles” rather than the plant proteins being integrated within the casein micelle. Applicant argued that the use of “in” in the phrase “stable suspension […] in a dairy product” recited by Jimenez refers to the dispersion of the protein within the liquid phase of the product, not the structural placement of glycinin within the interior of the micelle itself (Applicant’s Remarks, page 7, 1st paragraph under “Response to Claim Rejections Under 35 U.S.C. § 103” – page 9, 2nd paragraph).
However, Fig. 1 of Jimenez renders the claimed foreign particle in the interior of the structure obvious. "To support the conclusion that the claimed invention is directed to obvious subject matter, either the references must expressly or impliedly suggest the claimed invention." Ex parte Clapp, 227 USPQ 972, 973 (Bd. Pat. App. & Inter. 1985). MPEP §2142. Fig. 1 of Jimenez clearly depicts plant proteins in the middle of the micelle structure at the end of the process depicted in Fig. 1 (i.e., far right-side of Fig.1). Fig. 1 of Jimenez clearly labels this structure with plant proteins in the middle of the structure as being a “stable blend of casein and plant protein”. By labeling the structure in Fig. 1 as “stable blend of casein and plant protein”; describing the schematic of Fig. 1 as being a process for producing a stable blend of casein and plant proteins [0009]; describing casein micelles as being a unique system for blending with proteins [0026]; and disclosing that blending milk proteins with plant proteins using physical, chemical, and biochemical principles [0045], Jimenez demonstrates that its “stable blend” refers to the casein micelle containing the plant protein. Therefore, Jimenez at least suggests that the plant protein is in the core of the structure. Furthermore, Applicant stated in the 1st paragraph on page 8 of Applicant’s Remarks filed 10/23/2024 that one of the interpretations of Fig. 1 of Jimenez is that “the foreign particle is inside the core”, thereby admitting that Jimenez discloses an option wherein the plant protein is located within the interior of the casein micelle as presently claimed.
In response to Applicant’s assertion that the term “co-dispersion” means that the plant protein and casein micelles remain distinct, the prefix “co-“ literally means “together, with, or jointly” so that a “co-dispersion” means that at least two ingredients are associated with one another and those associated ingredients are dispersed within a substance while still associated with one another. Jimenez explicitly states that those at least two ingredients are the plant protein and casein micelle [0050]. Therefore, the plant protein and casein micelle are not physically distinct from one another.
In response to Applicant’s assertion that the use of “in” in the phrase “stable suspension […] in a dairy product” recited by Jimenez refers to the dispersion of the protein within the liquid phase of the product, not the structural placement of glycinin within the interior of the micelle itself, the protein being located within the interior of the casein micelle does not prevent the protein from being concurrently suspended within a dairy product.
In response to Applicant’s assertion that Table 2 and Fig. 6 of Jimenez show that the increase in casein micelle size is consistent with swelling of the micelle, not with internal incorporation of a secondary protein into the core of the micelle, Examiner agrees with this assessment as Jimenez clearly states that sodium citrate is used to swell the casein micelles prior to the addition of the proteins to the casein micelles (see the “distended Casein Micelle” shown in Fig. 1) which results in the incorporation of the proteins within the casein micelle (see the “Stable Blend of Casein and Plant Protein” shown in Fig. 1) (Fig. 1, [0005], [0014], [0049]).
Applicant then argued that there is no reasonable expectation of success of obtaining the claimed invention when combining the teachings of Jimenez with the teachings of Beliciu. Applicant argued that Beliciu provides empirical evidence that soy proteins and casein micelles do not interact in the manner required by the present claims as Beliciu explicitly states that heat treatment did not induce any chemical interactions between the soy proteins and casein micelles. Applicant argued that neither Jimenez nor Beliciu discloses a process which would cause soy glycinin to pass through the exterior layer of a casein micelle to enter the interior of the casein micelle in order to become embedded with the casein protein matrix of the interior of the micelle (Applicant’s Remarks, page 9, 3rd paragraph – page 10, 2nd paragraph; page 11, 2nd – 3rd paragraphs).
However, Beliciu is cited for its teaching regarding glycinin and soy globulin 7S and 11S being suitable soybean protein fractions for association with a casein micelle since Jimenez discloses the incorporation of soybean protein into its casein micelles (Jimenez, [0027], [0033]). Beliciu is not cited for its teachings regarding a method of incorporating glycinin into the interior of casein micelles as Jimenez already discloses a method of incorporating plant protein within the interior of casein micelles to form stable casein micelles. Therefore, the combination of Beliciu with Jimenez results in a stable casein micelle containing glycinin within the interior of the micelle. The test for obviousness is not whether the features of a secondary reference may be bodily incorporated into the structure of the primary reference; nor is it that the claimed invention must be expressly suggested in any one or all of the references. Rather, the test is what the combined teachings of the references would have suggested to those of ordinary skill in the art. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981).
Applicant then argued that a skilled practitioner would understand that there are multiple distinct physical states for a secondary protein in a casein micelle: continuous phase dispersion as taught by Beliciu; surface adsorption; layer intercalation; and structural incorporation as disclosed in present claim 1. Applicant argued that improper hindsight has been applied by reducing these complex physical states to a “finite number of predictable solutions” (i.e., inside or outside the micelle) (Applicant’s Remarks, page 10, 3rd paragraph – page 11, 1st paragraph).
However, the Examiner points out that the present claims do not require the glycinin to be entirely located within the interior of the micelle. Therefore, out of the four distinct physical states for a secondary protein in a casein micelle asserted by the Applicant, layer intercalation and structural incorporation are both encompassed by present claim 1, especially wherein the Applicant has not demonstrated in its examples which of the four asserted distinct physical states for a secondary protein in a casein micelle is displayed by the claimed invention.
Since Wolff states that the non-casein protein “can be part of the micelle” (page 15, lines 13-15), Wolff rules out continuous phase dispersion from the four distinct physical states for a secondary protein in a casein micelle asserted by the Applicant as “part of the micelle” means that the secondary protein has some physical incorporation with the casein micelle. Therefore, out of the four distinct physical states for a secondary protein in a casein micelle asserted by the Applicant, only three of them are actually options for Wolff. From this list of only three options, a skilled practitioner would still be able to “at once envisage” the soy protein being located in the interior of the micelle and thus, “at once envisage” the claimed arrangement to meet the claimed structure, especially wherein the encapsulation of non-milk proteins by casein micelles was known in the art at the time of the present filing as disclosed by Krentz II (Krentz et al., 2022, “Use of casein micelles to improve the solubility of hydrophobic pea proteins in aqueous solutions via low-temperature homogenization”, Journal of Dairy Science, 105, pages 22-31; previously cited) (page 23, 1st column , 2nd paragraph) and the encapsulation of hydrophilic macromolecules by casein micelles was known in the art at the time of the present filing as disclosed by Sadiq (page 2, 5th paragraph).
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Applicant then argued that the encapsulation described in Sadiq is a transient “host-guest” relationship wherein the micelle acts as a temporary delivery vehicle for a bioactive while the claimed invention is a permanent structural transformation. Applicant argued that the reliance on Sadiq’s encapsulation mechanism is technically incompatible with the teaching of Beliciu so that Sadiq is an improper reference from evidencing Beliciu (Applicant’s Remarks, page 11, 4th paragraph – page 12, 1st paragraph).
However, Sadiq was not used to evidence Beliciu; therefore, Applicant’s arguments regarding such are moot. Sadiq is used in the rejections as an evidentiary reference for Jimenez and Wolff in order to demonstrate the structure of the casein micelles disclosed in Jimenez and Wolff. Neither the method of Sadiq nor the method of Beliciu is cited or relied on in the rejections of the present claims and thus there is no issue of incompatibility between the two methods.
Furthermore, the present claims do not require the claimed structure to be stable for any period of time. Therefore, if the structure of the prior art remains stable for any period of time (e.g., 0.001 second), that structure meets the claimed limitation of being “stable”.
Since the prior art has been shown to render the present claims obvious and Applicant’s arguments regarding Jimenez, Wolff, Beliciu, and Sadiq have been shown to be unpersuasive, the rejections of the claims are maintained as written herein.
Double Patenting Rejections: Applicant did not provide any arguments against the double patenting rejections; therefore, the rejections are maintained as written herein.
Conclusion
THIS ACTION IS MADE FINAL. 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.
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/KELLY P KERSHAW/Examiner, Art Unit 1791