DETAILED ACTION
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 .
Continued examination under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e) was filed after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.114 has been timely paid, the finality of the previous Office Action has been withdrawn pursuant to 37 CFR 1.114. Applicant’s submission filed on 11/10/2025 has been entered.
Claim status
The examiner acknowledged the amendment made to the claims on 11/10/2025.
Claims 1, 3-12, 14-15, 17-21, 23-24 and 26-27 are pending. Claim 1 is currently amended. Claims 2, 13, 16 and 22 remain cancelled. Claims 25 and 28 are newly cancelled. Claims 15, 17-21 and 23-24 are withdrawn without traverse in response to the restriction requirement. Rest of claims are previously presented. Claims 1, 3-12, 14 and 26-27 are hereby examined on the merits.
Examiner Note
Any objections and/or rejections that are made in the previous actions and are not repeated below, are hereby withdrawn.
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.
Claims 1, 3-4, 6-7, 9-12, 14 and 26-27 are rejected under 35 U.S.C. 103 as being unpatentable over Klemmer, "Pea protein‐based capsules for probiotic and prebiotic delivery", International Journal of Food Science and Technology, 2011, 46, pages 2248-2256 (hereinafter referred to as Klemmer) in view of Yuuri JP2007068426 A (English translation relied upon for reference, hereinafter referred to as Yuuri), Lee US Patent Application Publication No. 2012/0161067 A1 (hereinafter referred to as Lee) and Batista, “Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques” 2005, 36, pages 135-143 (hereinafter referred to as Batista) .
Regarding claims 1, 3-4, 6-7, 11-12, 14 and 26-27, Klemmer teaches a method comprising the steps of (page 2250, left hand column, 1st para.):
- solubilizing pea protein isolate by mixing the pea protein with an alkali solvent (e.g., Milli-Q water the pH of which is adjusted to 10 by 1M NaOH) to provide a 6% solubilized pea protein solution (w/w);
-heating the pea protein solution at 80 ºC with constant stirring for 30 min; and
- cooling the protein solution to room temperature with water bath.
The pH of the alkali solvent as disclosed by Klemmer falls within the ranges recited in claims 1 and 3-4.
Klemmer teaches a 6% (w/w) pea protein, which is about 6% (w/v) thus falling within the range recited in claim 1 (assuming the density of the solution is 1 g/ml).
Klemmer teaches an alkali solvent (e.g., water mixed with 1M NaOH) but does not explicitly teach the molarity of the NaOH, however, given that the molarity of NaOH determines the pH of the solution and Klemmer teaches a pH of 10 that falls within the range of 10-11 as recited in the instant claim 4, and that the concentration of pea protein as disclosed by Klemmer is comparable to the claimed invention, it logically follows that the alkali solvent as disclosed by Klemmer has the molarity of 0.05-0.2 M as recited in claim 1.
Klemmer does not explicitly teach that up to 70% of the pea protein is solubilized by the mixing the pea protein with the alkali solvent, or that the pea protein is substantially but not fully solubilized in the alkali solvent. However, when the pea protein powder is dispersed in the alkali aqueous solution, majority of protein will dissolve and residual amount of protein will necessarily be left undissolved, which is interpreted to read on “substantially but not fully solubilizing pea protein”. Further, wherein prior art teaches the same step of mixing a pea protein with an alkali solvent having the same molarity or pH and the concentration of the pea protein solution falls within the range of 6-9% (e.g., 6%), it logically follows that up to 70% of the pea protein is solubilized by the mixing. See MPEP 2112.01 I, where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).
Klemmer is silent regarding resting the solubilized pea protein solution for 15 minutes- 2 hours (or at least 30 min as recited in claim 6, or at least 40 min as recited in claim 7, or 15-45 min as recited in claim 26, or 45 min as recited in claim 27) to further solubilize and hydrate the pea protein, and to provide a greater than 90% (w/v) solubilized and rested pea protein.
Yuuri teaches a method of solubilizing (e.g., extracting) pea protein comprising resting (e.g., leaving) the pulverized pea protein in alkali solution for 30 min to solubilize the protein (0028).
As such, before the effective filling date of the claimed invention, it is known to rest a solution that contains pea protein for some duration to solubilize the protein therein.
Both Klemmer and Yuuri are drawn to pea protein. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Klemmer by leaving to stand or resting the solution that contains pea protein for the purpose of solubilizing pea protein.
Regarding the duration of resting the pea protein solution: the duration of resting the pea protein solution is among the general conditions known by one of ordinary skill in the art to affect the proportion of the pea protein that is solubilized, given that solubilization is the interaction between a solute and a solvent. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have manipulated the duration of leaving the pea protein solution to stand so as to obtain a maximum or sufficient solubilization of the pea protein. Therefore, durations of resting as recited in claims recited in the claims 6-7 and 26-27 are merely obvious variants of the prior art. In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 “Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation”. (See MPEP 2144.05 II). Given the degree of solubilization for pea protein is a parameter of the resting time, the limitation about greater than 90% (w/v) solubilized pear protein is also obvious over the teaching of the prior art.
Given that prior art teaches the same resting step in alkali solution as that recited in the instant claim, it logically follows that this resting step will hydrate the pea protein.
Klemmer teaches heating the pea protein solution but is silent regarding heating the pea protein solution under conditions sufficient to heat-denature at least 90% of the pea protein. However, the specification teaches that "conditions sufficient to heat-denature the pea protein without causing gelation of the pea protein solution" means a temperature and time treatment that denatures at least 90%, 95% or 99% of the pea protein present in the solution while maintaining the solution in a form suitable for extrusion (i.e. readily flowable with suitable viscosity). The temperature and times employed may be varied depending on the concentration of the pea protein solution. Thus, for example, when an 8% pea protein solution (w/v) is used, the solution may be treated at a temperature of 80-90°C for 20-30 minutes (specification, page 11, lines 4-12). Example 1 and Example 4 of the specification further disclose heating an 8% pea and a 7% protein solution at a temperature of 85°C for 25 minutes such that the solution can be used for extrusion to prepare a microcapsule (specification, page 14 and page 16-17).
Klemmer as recited above, teaches heating 6% pea protein at 80 ºC for 30 minutes (page 2250, left hand column, 1st para.), the heating condition of which falls within the ranges recited in the specification for denaturing at least 90% of the pea protein while maintaining the solution in a form suitable for extrusion. Further, the 6% pea protein as taught by Klemmer is close to and a little bit lower than 7-8% pea protein as recited in the specification, and will reasonably result in similar or a little bit higher proportion of denatured pea protein under the same heating condition. As such, the heating step of Klemmer will necessarily serve the purpose or effect of heat-denature at least 90% of the pea protein.
Klemmer in view of Yuuri is silent regarding at least 90% or at least 95% the denatured protein solution is present as a soluble pea protein aggregate. However, since Klemmer in view of Yuuri teaches the same solubilizing, resting and heating steps as those recited in the instant claim, it logically follows that at least 90% of the pea protein in the pea protein solution as taught by Klemmer in view of Yuuri will be present as soluble pea protein aggregates if measured by the Shake Flask method.
Klemmer teaches cooling the pea protein solution by water bath, and further teaches a step of mixing the cooled pea protein solution with other components to form a mixture which is then extruded through a needle (page 2250, left hand column, 1st para.; page 2252, left hand column, first para. and Table 1). Klemmer is silent regarding preventing gelation by immediately and rapidly cooling the denatured pea protein solution to accelerate cooling and maintaining the solution in a form suitable for extrusion into microdroplet thereby providing a cooled denatured pea protein solution with a sufficiently low viscosity to permit the cooled denatured pea protein solution to be extruded or sprayed.
Lee teaches that in the process of extrusion through a needle, if the material that is being extruded is in the form of a gel that is too viscous, the material cannot be easily extruded from the syringe and might easily clog the needle and is thus inconvenient in practical operation ([0022]).
Batista teaches that the rate of cooling a denatured pea protein solution affects the gelation formation; in particular, pea protein solution that is not rapidly cooled (e.g., in a rheometer where the temperature drops 0.6 ºC/min) might form gel but if the pea protein solution is cooled in a refrigerator, no gel is formed (page 136, 2.2.1.1 and 2.2.1.3; page 138 right hand column, 3rd para.; page 139, left hand column, bottom para.).
Both Klemmer and Lee are directed to methods of extrusion using a needle/syringe. Both Klemmer and Batista are directed to cooling a denatured pea protein solution. Where Lee teaches that a gel formation that is very viscous cannot be easily extruded from the syringe and might easily clog the needle, Batista teaches that cooling a denatured pea protein at a normal rate might form gel but cooling it in a refrigerator will prevent gelation. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Klemmer by cooling the denatured pea protein solution in a refrigerator. Doing so would have prevented gelling of the pea protein thus the denatured pea protein would have been less viscous and would been suitable for extrusion through a needle. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have started the cooling process immediately after the heating so as to avoid the formation of gel. Where the cited arts in combination teach the same step of rapid cooling the heat-denatured pea protein solution to accelerate cooling, it logically follows that the resulted rapidly cooled denatured protein solution is in a form suitable for extrusion into microdroplets. See MPEP 2112.01 I, where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).
Regarding claim 9, Klemmer teaches that the pea protein comprises a source of pea protein having a purity of 80.01% (page 2249, right hand column, para.1), which falls within the purity value recited in the claim.
Regarding claim 10, Klemmer, as recited above, teaches that the pea protein is pea protein isolate (page 2250, left hand column, 1st para.).
Claim 5 is rejected under 35 U.S.C. 103 as being unpatentable over Klemmer in view of Yuuri, Lee and Batista as applied to claim 1 above, and in further view of Schweizer US Patent Application Publication No. 2013/0287928 A1 (hereinafter referred to as Schweizer).
Regarding claim 5, Klemmer in view of Yuuri, Lee and Batista teaches what has been recited above but is silent regarding the pea protein is centrifuged to remove insoluble matter. Schweizer teaches removing insoluble material from a protein solution by centrifugation so as to provide a clarified protein solution for further processing ([0039]). Both Klemmer and Schweizer are directed to processing protein solutions. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Klemmer by including the step of removing insoluble material from the protein solution by centrifugation to provide a clarified protein solution for further processing.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Klemmer in view of Yuuri, Lee and Batista as applied to claim 1 above, and further in view of Hayakawa US Patent Application Publication No. 2008/0213758 A1 (hereinafter referred to as Hayakawa).
Regarding claim 8, Klemmer in view of Yuuri, Lee and Batista teaches what has been recited above but is silent regarding the pea protein is solubilised by sonication in which the pea protein is dispersed in deionized water, phosphate or borate buffer prior to sonication. Hayakawa teaches a method of dissolving wheat protein by dispersing (e.g., suspending) wheat protein in a phosphate buffer followed by an ultra-sonication step to dissolve the protein ([0094]). Both Klemmer and Hayakawa are directed to dissolving plant proteins. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Klemmer by applying the ultra-sonication procedure as taught by Hayakawa to dissolve the pea protein.
Response to Arguments
Applicant's arguments filed 11/10/2025 have been fully considered but they are not persuasive.
Applicant argues on page 7 of the Remarks that Klemmer teaches using 1 M NaOH for solubilization of the pea protein, thus failing to teach the limitation about an alkali solvent comprising an aqueous solution of 0.05 M to 0.2 M base. Applicant further argues that since Klemmer does not teach the molarity of a base as recited in claim 1, the limitation about up to 70% of the pea protein being solubilized is not taught by Klemmer. Applicant further argues that it is for this reason that Klemmer does not employ a resting step. Applicant further argues that the use of a high strength of alkali solvent would damage the pea protein.
The argument is considered but found unpersuasive. Klemmer teaches solubilizing pea protein isolate by mixing the pea protein with an alkali solvent (e.g., Milli-Q water the pH of which is adjusted to 10 by 1M NaOH) to provide a 6% solubilized pea protein solution (w/w), thus given that the molarity of NaOH determines the pH of the solution and Klemmer teaches a pH of 10 that falls within the range of 10-11, and that the concentration of pea protein as disclosed by Klemmer is comparable to the claimed invention, it logically follows that the alkali solvent as disclosed by Klemmer has the molarity of 0.05-0.2 M as recited in claim 1.
For the reason set for the above, applicant’s arguments about Klemmer failing to teach the limitation of solubilizing up to 70% pea protein, about Klemmer intentionally skipping resting step and about the pea protein of Klemmer being damage by the strong alkali are not persuasive, either.
Regarding Yuuri, applicant argues on page 7 of the Remarks that Yuuri describes a single solubilization only (e.g., the resting step) and does not describe the step of mixing protein with an alkali solvent to provide 6-9% solubilized pea protein.
The argument is considered but found piecemeal. While Yuuri does not disclose all the features of the present claimed invention, Yuuri is used as teaching reference, and therefore, it is not necessary for this secondary reference to contain all the features of the presently claimed invention, In re Nievelt, 482 F.2d 965, 179 USPQ 224, 226 (CCPA1973), In re Keller 624 F.2d 413, 208 USPQ 871, 881 (CCPA 1981). Rather this reference teaches a certain concept, namely, resting a solution that contains pea protein for some duration would help to solubilize the protein therein, and in combination with the primary reference, discloses the presently claimed invention. Further, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck &Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).
All the arguments on page 8 of the Remarks regarding Cho are acknowledged, but irrelevant to the instant office action, since Cho is no longer relied upon.
Applicant argues on page 8 of the Remarks that Klemmer does not teach heating a rested pea protein solution.
The argument is considered but found piecemeal because the rejection is not over Klemmer alone. In the instant case, Klemmer in view of Yuuri teaches heating a rested pea protein solution. Note that where Klemmer teaches heating a solution with dissolved protein (see page 2250), the heating step as in Klemmer in view of Yuuri necessarily occurs after the resting step that serves to further solubilize the pea protein.
Applicant argues on pages 8-9 of the Remarks that Klemmer teaches mixing alginate with the pea protein solution, and that the skilled person has no motivation to investigate the use of the intermediate solution of Klemmer (e.g., pea protein solution without alginate) to form a cooled denatured pea protein solution suitable for being extruded. Applicant further argues that even if the skilled person were to consider this intermediate solution, the solution would be unsuitable for the purpose due to the foaming and viscosity issue as applicant has raised. Applicant goes to argue that the skilled person would not stop the Klemmer synthesis and investigate the intermediate solution with an expectation of arriving at the claimed process to provide a pea solution that can be extruded.
The arguments are considered but found unpersuasive. For the record, Klemmer teaches cooling the heated pea protein solution before adding alginate (see page 2250, left hand column, first para.), not cooling a solution of a mixture comprising pea protein and alginate. Nor does claim 1 actively recites an extrusion step, rather, claim 1 merely recites that the pea protein solution as recited is suitable for extruding as a result of solubilizing in an akala solvent, resting and rapid cooling. Further, applicant is reminded that the instant claim 1 does not include a negative limitation that excludes alginate, nor does the disclosure as originally filed have the support for such a negative limitation. To this end, applicant is respectively invited to refer to para. 6-7 of the OA issued 11/14/2020 for parent application 15/536,303, in which the examiner submits that the negative limitation that the alginate is not present in the pea protein solution is not sufficiently supported by the disclosure as originally filed.
Further the arguments have overlooked that the rejection is not over Klemmer alone, but over Klemmer as modified by Yuuri, Lee and Batista. The arguments have failed to address the merits of the rejection because applicant did not address the motivations the office action has provided that would suggest one of ordinary skill in the art to make the proposed modifications. In the instant case, the motivation to modify Klemmer with Yuuri lies in that resting the alkali pea protein solution will deliver the benefit of further solubilizing the pea protein, and the motivation to modify Klemmer with Lee and Batista is that rapidly cooling the heat-treated pea protein solution will deliver the benefit of preventing gelling of the pea protein thus the denatured pea protein would have been less viscous and would been suitable for extrusion through a needle. Further, Klemmer as modified by Yuuri, Lee and Batista arrives at the claimed invention and will not have the issue of foaming and viscosity, since resting will eliminate foaming and rapid cooling will not cause viscosity to increase.
Further, it does not appear that modification of Klemmer with Yuui, Lee and Batista will stop the Klemmer synthesis and use the pea protein solution without alginate for extruding, for the reason that Klemmer as modified by Yuuri, Lee and Batista merely results in a cooled pea protein solution the pea protein of which is not gelled or is less viscous, and the step of adding alginate to the cooled pea protein solution would not be interrupted.
Conclusion
Pertinent art
The prior art made of record and not relied upon is considered pertinent to applicant’s disclosure
Abayomi, “Functional properties of protein fractions obtained from commercial yellow
field pea (Pisum sativum L.) seed protein isolate”, Food Chemistry, 2011, 128, pages 902-908, which teaches solubilization of pea protein isolate by dispersing pea protein isolate in 0.1 M NaOH (section 2.6).
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/CHANGQING LI/Primary Examiner, Art Unit 1791