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 .
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 32-34, 36-38 and 45-46 are rejected under 35 U.S.C. 103 as being unpatentable over Zhang et al. (US 2021/0092977 A1) in view of Hu et al. “Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments”, hereon referred to as “Hu”.
Regarding claim 32, the limitation “high-intensity ultrasound waves” is interpreted in view of the specification to have a frequency between 20-100 kHz and a power between 5-50 W/cm2 (page 3 lines 7-12).
Zhang et al. teaches a method for producing a concentrated liquid protein (abstract), the protein sourced from plants, including lupin (paragraphs 45 and 47), comprising separator 110, ultrasonicator 120, filtration unit 130 and dryer 140 (paragraph 23), where protein base is mixed with water at a weight ratio of 1:5 to 1:20 to form a solution (paragraph 23), passed through the separator 110 to remove fibrous material and obtain a concentrated protein base (solution of lupin protein concentrate) before ultrasonication (paragraph 24), subjecting the separated protein base to ultrasonication (paragraph 25), filtering the ultrasonicated protein base in filtration unit 130 (paragraph 27), then drying in dryer 140 to obtain the protein ingredient i.e., collecting the modified protein to form a protein feedstock (paragraph 29).
Regarding the ultrasound being “high-intensity ultrasound waves”, the reference teaches ultrasonication is performed at a frequency of up to 20 kHz at a power in the range from 100-400 W for 15 minutes or longer (paragraph 42), where parameters such as amplitude, flow rate, power density, and/or duration are controlled based on desired characteristics of the protein such as extractability, viscosity, dispersion and de-foaming (paragraph 41). The reference recites an example where the power density is 50-100 W/ml at 20 kHz (paragraph 73).
Zhang et al. does not explicitly recite the disclosed ranges of frequency and power as interpreted above.
Hu et al. teaches high-intensity ultrasonic pre-treatments of soybean protein isolate (SPI) improve water holding capacity, gel strength and firmness of SPI gels (abstract), the high-intensity ultrasound having a frequency of 16-100 kHz and a power in the range of 10-1,000 W/cm2 (page 187 section 1 first paragraph), where the process comprises forming a solution of SPI in distilled water prior to exposure to the ultrasound (page 188 section 2.2).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. to use the disclosed ranges since the prior art contemplates adjusting such parameters based on the characteristics of the protein base and/or final protein product, since the prior art recognizes using high-intensity ultrasound having the claimed parameters to treat protein material, since there is no evidence of criticality or unexpected results associated with the features and ranges, and since the values would have been used during routine experimentation and optimization due to factors such as those stated above.
Zhang et al. does not specify that the ultrasonication forms a modified protein having a decreased thermal stability compared to unmodified lupin protein.
Hu et al. teaches high intensity ultrasound causes changes in characteristics of protein, such as solubility and apparent viscosity, altered flow behavior, and rheological properties, and facilitates food protein heat-induced gelation i.e., decreased thermal stability (page 187 section 1 second and third paragraphs). High-intensity ultrasound is disclosed to unfold proteins and result in structural changes (page 191 left column).
Since the combination of Zhang et al. and Hu et al. above teaches high-intensity ultrasonication of lupin protein using ultrasound parameters disclosed by Applicant, and since high-intensity ultrasonication is recognized to cause changes in proteins, absent evidence to the contrary, one of ordinary skill in the art would have reasonably expected similar protein modification and decreased thermal stability in the lupin protein of Zhang et al.
Zhang et al. does not teach the lupin protein concentrate has a purity greater than 65% prior to ultrasound treatment.
However, the reference teaches separator 110 removes fibrous and non-protein materials from the protein base prior to ultrasonication, thereby preventing clogging of the membrane filter in unit 130 and minimizing necessary pressure applied (paragraph 24). Further, a solution made from only lupin would necessarily have a lupin protein purity of 100% since the lupin is the sole source of protein.
Hu et al. further teaches soybean protein isolate (SPI) is subjected to the high-intensity ultrasound, where one of ordinary skill would understand that isolates of a particular type of protein would necessarily have high purity of said protein type.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. to use lupin protein concentrate having the claimed purity since the prior art already recognizes subjecting concentrated lupin protein obtained by separation of non-protein materials to ultrasound waves, to minimize clogging and required pressure for later filtration, since there is no evidence of record that the claimed purity of lupin protein provides unexpected results, and since the claimed values would have been used during routine experimentation and optimization procedures due to factors such as degree of non-protein material separation, and the type of protein concentrate used for ultrasonication.
Zhang et al. teaches ultrasonication at temperatures lower than 85oC (paragraph 25), but does not specify maintaining the solution below about 35oC.
Hu et al. further teaches sonication while holding the solution in an ice-bath to maintain the temperature of the solution below 2oC (page 188 section 2.2). The ultrasonication is recognized to produce heat (page 188 section 2.3), where an increase in temperature can lead to aggregation of the proteins (page 190 section 3.1).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. to maintain the temperature below 35oC during ultrasonication since the prior art recognizes a desire to maintain a reduced temperature during said process, in order to ensure the solution does not overheat and denature due to generation of heat during ultrasonication, since there is no evidence indicating criticality or unexpected results associated with the claimed values, and since the values would have been subjected to routine experimentation and optimization due to factors such as the degree of ultrasonication applied, and degree of denaturing and/or agglomeration of the proteins.
Zhang et al. does not teach the solution of protein is exposed to ultrasound at a pH of about 7.0.
However, the reference teaches the protein containing source material is mixed with a significant portion of water e.g., at a weight ratio of 1:5 to 1:20 (paragraph 23).
Hu et al. further teaches the process comprises forming a solution of SPI in distilled water prior to exposure to the ultrasound (page 188 section 2.2).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. such that the protein solution has a pH of “approximately 7.0” since the solution comprises mostly water, since there is no evidence indicating criticality or unexpected results associated with the claimed pH, and therefore one of ordinary skill would have reasonably expected a solution comprising mostly water to be “approximately 7.0”, and since the pH would have been subject to experimentation and optimization due to factors such as the composition of the solution of protein, specifically the amount of water present therein.
Regarding claim 33, the combination applied to claim 32 does not teach the modified lupin protein has an increased proportion of beta-sheets compared to unmodified protein.
However, the combination applied to claim 32 teaches exposing a solution of purified lupin protein to high-intensity ultrasound waves as stated above, where the treatment is recognized to cause changes to the protein structure. The increased proportion of beta-sheets is construed to be a feature inherent to the high-intensity ultrasonication process. Absent evidence to the contrary, one of ordinary skill would have expected the ultrasonicated lupin protein to have increased beta-sheets as claimed.
Regarding claim 34, the combination applied to claim 32 teaches and renders obvious high-intensity ultrasound waves having the claimed frequency and power values.
Regarding claim 36, Zhang et al. teaches ultrasonication is applied for a desired period of time such as 15 minutes (paragraph 42).
Regarding claim 37, Zhang et al. does not teach the solution of lupin protein has a protein concentration of about 10 wt%.
However, the reference teaches separation of non-protein materials from the solution of protein in separator 110, and Hu et al. teaches using protein isolates as the protein source as stated for claim 32. Further, the ratio of material to water can be adjusted as taught by Zhang et al. (paragraph 23).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. such that the protein concentration of the solution is about 10 wt% since the prior art recognizes ultrasonication of a concentrated protein solution, since there is no evidence of criticality or unexpected results associated with the claimed values, and since the values would have been subjected to routine experimentation and optimization due to factors such as the degree of separation prior to ultrasonication, amount of water used to form the solution, and type of protein material used (e.g., concentrate, isolates, etc.).
Regarding claim 38, the claim recites alternatives. For the sake of examination, the alternative “to purify the modified lupin protein after passing the high-intensity ultrasound waves through the solution” is chosen.
Zhang et al. teaches filtration unit 130 filters the ultrasonicated protein to increase the concentration thereof (paragraph 29), construed to be a type of purification process.
Regarding claims 45-46, Zhang et al. teaches the modified protein is isolated (paragraphs 16 and 19), the water is removed from the solution (paragraph 29) and collected as a powder (paragraphs 1 and 35).
While the reference does not explicitly teach the isolate having a content of 90% or more as recited in the specification (page 4 lines 29-30), it would have been obvious to one of ordinary skill in the art before the effective filing date of the to control the concentration and drying processes of Zhang et al. to obtain the claimed protein content since protein isolate powders are known, since there is no evidence of criticality or unexpected results associated with the claimed values, and since the values would have been subjected to routine experimentation and optimization due to factors such as degree of purification and water removal.
Claims 39-44 are rejected under 35 U.S.C. 103 as being unpatentable over Zhang et al. in view of Hu et al. as applied to claim 32 above, and further in view of Vrljic et al. (US 2019/0116855 A1).
Regarding claims 39-41, Zhang et al. does not teach adjusting a pH of a solution of modified lupin protein, after ultrasonication and prior to collecting, to an isoelectric point of said modified protein (claim 39), the pH being 4.5 (claim 40).
Vrljic et al. teaches isolated and purified proteins can be isolated based on their surface charge by isoelectric precipitation (paragraph 122), where the pH adjustment can be performed with acid on a solution of the protein (paragraph 157), and targeted proteins can be separated by isoelectric precipitation (paragraph 355). The proteins include lupin proteins and the pH is between 3.5 and 5.5 (paragraphs 48-49).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. to adjust the pH of the protein solution to the isoelectric point since the process of isoelectric precipitation is known in the art, since the prior art recognizes performing said process on lupin protein, and to further isolate specific lupin proteins based on desired characteristics, where the pH would have been subjected to routine experimentation and optimization based on the desired protein to be isolated/precipitated.
Zhang et al. suggests gelatinization (paragraph 59) but does not teach heating the solution comprising the modified protein to a temperature to induce aggregation and then cooling the solution to form a gel, where the temperature is above 70oC (claim 41).
Vrljic et al. teaches the proteins can be formed into gels by heating to above 70oC for stabilizing interactions (induced aggregation) and then cooling to room temperature (paragraph 155), where the gels can be used with other materials such as heat-labile components to form a food product such as meat replicas (paragraph 159).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. to gel the solution of modified protein by heating and cooling as claimed since the process is known for producing gelled foods, to allow for the incorporation of heat-labile components to form meat replicas, since there is no evidence of criticality or unexpected results associated with the claimed feature, where the temperature values would have been subjected to routine experimentation and optimization based on the particular protein used and desired characteristics of the final product.
Regarding claim 42, Zhang et al. does not teach the solution is maintained at the temperature for 60 minutes or less.
Vrljic et al. teaches various factors such as protein concentration, pH, and temperature contribute to the rate of gel formation and quality of the final product (paragraph 154), where the factors can be varied as stated for claims 39-41 above.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to modify the process of Zhang et al. to maintain the temperature for 60 minutes or less since the prior art recognizes gelling rate and duration depends on various factors, since there is no evidence of criticality or unexpected results associated with the claimed feature, since the modified protein solution of the prior art combination applied to claim 39 appears to be the same as that of the claimed solution, and therefore one of ordinary skill would have reasonably expected similar gelling properties, and since the claimed duration would have been subjected to routine experimentation and optimization based on the factors taught by Vrljic et al.
Regarding claim 43, the combination applied to claim 39 teaches cooling to room temperature as stated above.
Regarding claim 44, the combination applied to claim 39 teaches adjusting the pH of a solution of modified lupin protein. The solution comprising the modified lupin protein would have necessarily been formed prior to adjusting the pH of said solution.
Response to Arguments
The objection of claim 32, rejections of claims 32 and 38-39 under 35 USC 112(b), and rejection of claim 44 under 35 USC 112(d) are withdrawn in view of the respective amendments and cancelation of claim 44.
Applicant's arguments filed 3/27/2026 have been fully considered but they are not persuasive.
Applicant argues Zhang is directed to producing a clean-tasting, neutral-color, liquid protein base with improved characteristics, where Zhang’s use of ultrasonication is limited to physical and sensory improvements, the reference does not teach or suggest modifying protein structure to decrease thermal stability, and does not teach or contemplate enabling gel formation in proteins that otherwise cannot gel due to high intrinsic thermal stability. Applicant argues the claimed method forms modified lupin protein having decreased thermal stability relative to unmodified lupin protein to enable gel formation.
This is not persuasive since the reference teaches applying ultrasonication to lupin protein in order to obtain characteristic changes (i.e., modification) in the protein (paragraph 41), where the parameters of the process are controlled to obtain the desired characteristics. The ultrasonication uses parameters disclosed by Applicant (i.e., 20 kHz frequency at a power range of 100-400W for 15 minutes, where controlled parameters include amplitude, powder density and/or duration, and an example powder density is 50-100 W/ml (paragraph 73). Further, Hu teaches high-intensity ultrasonic treatment of plant protein at frequencies and power values overlapping the ranges disclosed by Applicant, where the treatment improves water holding capacity, gel strength, and firmness of gels (abstract). While a decrease in thermal stability is not explicitly recited, one of ordinary skill would have reasonably expected treatment of purified lupin protein using the same high-intensity ultrasonic waves to obtain results similar to those argued. Additionally, Applicant’s specification discloses that cavitation phenomena from ultrasound treatment causes changes in protein structure (page 6 lines 13-15 and 23-25), which appears to be the same method of modification as the cited prior art. Additionally, Examiner notes that the argued feature of gel formation is not required by claim 32.
Applicant argues Zhang teaches ultrasonication conditions incompatible with the claimed method since the treatment is disclosed to be performed at a temperature of 100-140oF, well above the claimed temperature of below 35oC. Applicant argues the claimed temperature range ensures protein is modified without premature aggregation, allowing subsequent gel formation, and Zhang does not recognize such a problem.
This is not persuasive since the temperature range of the working example is a preferred embodiment. See MPEP 2123. The reference does not teach or otherwise indicate the ultrasonication must be performed at the disclosed temperature range (see whole document). Rather, the reference suggests that treatment can be performed below 85oC (paragraph 25). Further, Hu as applied to claim 32 teaches that it is desirable to perform sonication while maintaining the protein solution at a temperature below 35oC since the treatment is recognized to produce heat, where an increase in temperature leads to aggregation of the proteins (page 188 sections 2.2-2.3; page 190 section 3.1). Therefore, one of ordinary skill in the art would have been motivated to reduce the operating temperature of Zhang during ultrasonication in order to similarly minimize the risk of premature aggregation.
Applicant argues Zhang operates with protein concentrations that are dramatically lower than the claimed purity of greater than 65%, such as ratios of 1:5 to 1:20 with water, thus teaches away from the claimed process, and Zhang’s approach to use dilute protein slurries during ultrasonication and then concentration afterwards through membrane filtration is the opposite of the claimed method.
This is not persuasive since the disclosed ratios are preferred embodiments. The reference states “e.g., at 1:5 to 1:20 weight ratio” (paragraph 23). The reference does not teach or otherwise indicate the concentration of protein in the solution cannot be lower than 1:5. Rather, the reference teaches separation/filtration for “removing starch and other non-protein components may increase the resulting protein concentration in the concentrated protein base” (paragraph 24) prior to ultrasonication of said protein base (paragraph 25). This suggests to one of ordinary skill that the protein base can be concentrated to higher protein content or “purity” as claimed. Further, the evidence of record does not indicate criticality associated with the claimed purity of greater than 65%, particularly since it is not clear from the examples what purity value(s) were used.
Applicant argues Hu is directed exclusively to soybean protein isolate which has fundamentally different structural and thermal properties from lupin protein, whereas lupin proteins have weak gelation properties and higher thermal stability compared to soybean and pea proteins, and therefore the properties of lupin protein does not allow techniques developed for soybean protein to be simply applied to lupin protein with any reasonable expectation of success. Applicant argues Hu’s use of low temperatures during sonication is disclosed solely in the context of soybean protein, which possesses inherent gel-forming capabilities that lupin protein lacks, and the reference does not teach or suggest treatment decreases thermal stability.
This is not persuasive since Zhang already teaches ultrasonication of lupin protein, where the treatment causes cavitation, acknowledged by Applicant to cause modification as explained above. Hu is relied on to show that high-intensity ultrasonic treatment is recognized by the prior art to cause changes in protein structure. While lupin protein may have weak gelation properties and higher thermal stability compared to soybean and pea proteins, the prior art nonetheless recognizes protein modification and heat-induced gelation (i.e., decreased thermal stability) via ultrasonication. Absent evidence to the contrary, one of ordinary skill in the art would have expected applying high-intensity ultrasound to lupin protein as disclosed by Zhang to provide similar results.
Applicant argues the cited references do not provide articulated motivation to modify Zhang’s process to intentionally decrease lupin protein thermal stability, does not teach application of ultrasound to high-purity lupin protein concentrate under sub 35oC conditions, and there is no reasonable expectation that the combined teachings would enable gel formation in lupin protein, where the combination relies on impermissible hindsight.
This is not persuasive for the reasons stated above. While reduction of thermal stability in lupin protein is not explicitly taught by Zhang, the prior art recognizes high-intensity ultrasound provides cavitation to cause physical changes to protein structure. Likewise, Hu teaches maintaining temperature below 35oC during ultrasonication provides the advantage of preventing premature agglomeration, which provides motivation for one of ordinary skill to modify the process of Zhang.
Applicant’s argument against the dependent claim is not persuasive for the same reasons stated above.
Conclusion
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 BRYAN KIM whose telephone number is (571)270-0338. The examiner can normally be reached 9:30-6.
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/B.K/Examiner, Art Unit 1792
/ERIK KASHNIKOW/Supervisory Patent Examiner, Art Unit 1792
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