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 07/06/2026 is acknowledged.
Applicant has overcome the following rejections by virtue of the amendment or cancellation of the claims and/or persuasive remarks: the 35 U.S.C. §112(b) rejections of claims 6-8 and 16-24 have been withdrawn.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 6-8, 16-26
Withdrawn claims: None
Previously cancelled claims: 1-5, 9-15
Newly cancelled claims: None
Amended claims: 6, 8
New claims: 25-26
Claims currently under consideration: 6-8, 16-26
Currently rejected claims: 6-8, 16-26
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 6-8, 16-21, and 24-26 are rejected under 35 U.S.C. 103 as being unpatentable over Etzel (US 2009/0068326; previously cited) in view of Elgar (Elgar et al., “Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high performance liquid chromatography on polystyrene-divinylbenzene”, 2000, Journal of Chromatograph A, 878, pages 183-196; previously cited) and Vincent (Vincent et al., “Quantitation and Identification of Intact Major Milk Proteins for High-Throughput LC-ESI-Q-TOP MS Analysis”, 2016, PLoS ONE, 11(10); IDS citation) as evidenced by Yadav (Yadav et al., “Cheese whey: A potential resource to transform into bioprotein, functional/nutritional proteins and bioactive peptides”, 2015, Biotechnology Advances, vol. 33, pages 756-774; previously cited).
Regarding claims 6, 24, and 25, Etzel teaches a method for producing a whey protein fraction (corresponding to a whey protein isolate) wherein at least 90 wt.% of the total solids in the whey protein isolate are β-lactoglobulin and α-lactalbumin [0015]. Etzel teaches that the method comprises the step of: (i) providing a whey protein fraction from cheesemaking [0021]. Whey produced from cheesemaking comprises a mixture of different individual whey proteins including the β-casein derived proteose peptones PP8 fast, PP8 slow, and PP-5 (corresponding to component 8-fast, component 8-slow, and component 5, respectively) as evidenced by Yadav (page 764, column 1, paragraph under “4.2 Individual whey protein components”; page 765, column 1, paragraph under “4.2.7 Proteose-peptone component”); therefore, the provided whey protein fraction of Etzel contains at least one A1 β-casein derived proteose peptone selected from the list recited in present claim 6.
Etzel teaches that the provided whey protein fraction is subjected to gel filtration (corresponding to ion exchange using gel beads [0035] and optionally, subsequent gel filtration [0102]) to produce the whey protein fraction wherein at least 90 wt.% of the total solids in the whey protein fraction are β-lactoglobulin and α-lactalbumin [0015]. Since the filtered whey protein fraction contains at least 90 wt.% β-lactoglobulin and α-lactalbumin based on the total solids in the filtered whey protein fraction, the A1 β-casein derived proteose peptone content in the filtered whey protein fraction is at most 10 wt.% based on the total protein in the whey protein fraction. As such, Etzel teaches step (ii) of reducing the A1 β-casein derived proteose peptone content in the whey protein fraction of step (i) to a concentration which falls within the claimed concentration based on total protein in the whey protein fraction, thereby forming a reduced whey protein fraction. Since Etzel teaches steps (i) and (ii) of the method of present claim 6, it also teaches that the method produces a whey protein fraction having a reduced A1 β-casein derived proteose peptone as recited in present claim 6.
Furthermore, since the A1 β-casein derived proteose peptone content in the filtered whey protein fraction of Etzel is at most 10 wt.% based on the total protein in the whey protein fraction, the concentration of the at least one A1 β-casein derived proteose peptone selected from the group consisting of PP8 fast, PP8 slow, and PP-5 in the whey protein fraction after the reducing step is at most 10 wt.%. This concentration range of “at most 10 wt.%” falls within the concentration recited in present claim 6; and encompasses the concentration recited in present claim 24. It would have been obvious to one of ordinary skill in the art to select any portions of the disclosed ranges including the instantly claimed ranges from the ranges disclosed in the prior art references, particularly in view of the fact that; "The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set percentage ranges is the optimum combination of percentages" In re Peterson 65 USPQ2d 1379 (CAFC 2003). Also In re Malagari, 182 USPQ 549,533 (CCPA 1974) and MPEP 2144.05.I.
Etzel also teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104]. Therefore, Etzel teaches step (a) of claim 6 of providing a dairy-based product to be analyzed. Etzel does not teach steps (b)-(c) of the method as recited in present claim 6; or teach that step (c) comprises intact protein analysis and deconvolution as recited in present claim 25.
However, Elgar teaches that the most common method for analyzing whey proteins is liquid chromatography (LC), particularly high-performance liquid chromatography (HPLC) such as reversed-phase (RP) HPLC (page 184, column 1, 2nd paragraph). Elgar teaches that RP-HPLC can be coupled with electrospray ionization mass spectrometry (ESI-MS) for a more complete separation of major whey proteins such as proteose peptones with good recovery and suitable for quantitation (abstract; page 184, column 1, 3rd paragraph). Therefore, Elgar discloses step (b) of the claimed method.
It would have been obvious for a person of ordinary skill in the art to have modified the method of Etzel to include subjecting a whey protein fraction to LC-MS analysis as taught by Elgar. Since Etzel teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104], a skilled practitioner would be motivated to consult Elgar to determine a suitable known method of determining and quantifying the proteins in the whey protein fraction of Etzel. In consulting Elgar, the skilled practitioner would readily recognize that RP-HPLC is a known method of quantifying milk proteins including proteose peptones comprising PP8 fast, PP8 slow, and PP-5 and that this known method may be coupled with ESI-MS in order to optimize the quantification process. Therefore, the combination of Etzel and Elgar renders subjecting a whey protein fraction to LC-MS analysis as recited in step (b) of present claim 6 obvious.
The combination of Etzel and Elgar does not teach step (c) of the method as recited in present claim 6; or teach that step (c) comprises intact protein analysis and deconvolution as recited in present claim 25.
However, Vincent teaches that determination and quantification of components by LC and MS are performed by detecting compounds of defined m/z values (corresponding to detecting bCN in the milk samples using the defined m/z values of bCN standards); and deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses (page 12, 2nd paragraph; page 16, Fig. 4, Panels F and H; pages 23-24, section labeled “1.2. Mass spectrometry”). Vincent also teaches that the preparation of milk samples for intact protein analysis has been well established (page 3, 3rd paragraph), thereby disclosing that intact milk protein analysis using LC-MS is well established in the art. Therefore, Vincent discloses step (c) of the claimed method.
It would have been obvious for a person of ordinary skill in the art prior to the effective filing date of the present invention to have modified the method of modified Etzel to include performing step (c) by intact protein analysis and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as taught by Vincent. Since (A) Elgar teaches LC-MS analysis as a method of determining and quantifying proteins (page 184, column 1, 2nd paragraph); and (B) Vincent teaches that LC-MS analysis comprises deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses (page 12, 2nd paragraph; page 16, Fig. 4, Panels F and H; pages 23-24, section labeled “1.2. Mass spectrometry”), a skilled practitioner would readily recognize that the method of modified Etzel comprises deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses as recited in step (c) of present claim 6 and as recited in present claim 25. Furthermore, the practitioner would recognize that the step may further comprise intact protein analysis as recited in step (c) of present claim 6 and as recited in present claim 25 since Vincent discloses that intact protein analysis coupled with LC-MS is known in the art. The combination of Elgar and Vincent yields predictable results as this combination represents the combining of prior art elements according to known methods. MPEP §2143.I.A. Therefore, the combination of prior art renders claims 6 and 25 obvious.
Regarding claim 7, Etzel teaches the invention as described above in claim 6, including reducing the content of the at least one A1 β-casein derived proteose peptone comprises gel filtration of the whey protein fraction (corresponding to ion exchange using gel beads [0035] and optionally, subsequent gel filtration [0102]) of the whey protein fraction.
Regarding claims 8 and 26, Etzel teaches a method for producing a nutritional composition (corresponding to foodstuffs, protein supplement, pharmaceutical formulation, or therapeutic application) containing a whey protein fraction (corresponding to a whey protein isolate), wherein at least 90 wt.% of the total solids in the whey protein fraction are β-lactoglobulin and α-lactalbumin [0014]-[0015]. Etzel teaches that the whey protein fraction is whey from cheesemaking that has undergone gel filtration (corresponding to ion exchange using gel beads and optionally, subsequent gel filtration) [0021], [0035], [0102]. Whey produced from cheesemaking comprises a mixture of different individual whey proteins including the β-casein derived proteose peptones PP8 fast, PP8 slow, and PP-5 (corresponding to component 8-fast, component 8-slow, and component 5, respectively) as evidenced by Yadav (page 764, column 1, paragraph under “4.2 Individual whey protein components”; page 765, column 1, paragraph under “4.2.7 Proteose-peptone component”); therefore, the provided whey protein fraction of Etzel contains at least one A1 β-casein derived proteose peptone selected from the claimed list. Etzel teaches that the whey from cheesemaking is subjected to gel filtration [0035], [0102] in order to produce the whey protein fraction wherein at least 90 wt.% of the total solids in the whey protein fraction are β-lactoglobulin and α-lactalbumin [0015]. Since the whey protein fraction contains at least 90 wt.% β-lactoglobulin and α-lactalbumin based on the total solids in the whey protein fraction, the A1 β-casein derived proteose peptone content in the whey protein fraction is at most 10 wt.% based on the total protein in the whey protein fraction. Therefore, Etzel teaches that the whey protein fraction is a reduced whey protein fraction having a reduced A1 β-casein derived proteose peptone content and teaches step (i) of providing a whey protein fraction and step (ii) of selecting the whey protein fraction having at most 10 wt.% of A1 β-casein derived proteose peptone based on the total protein in the whey protein fraction, forming a selected whey protein fraction as presently claimed. Etzel then teaches that the method comprises step (iv) of preparing a nutritional composition with the selected whey protein fraction [0014] as presently claimed. Since Etzel teaches the claimed method, Etzel teaches a method for producing a nutritional composition having a reduced -casein derived proteose peptone content as presently claimed.
Etzel also teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104]. Therefore, Etzel teaches step (ii) of claim 8 of determining and quantifying A1 β-casein derived proteose peptone (as a consequence of determining and quantifying the amount of whey in the whey protein fraction); and step (a) of claim 8 of providing a dairy-based product to be analyzed.
Etzel does not teach steps (b)-(c) of the method as recited in present claim 8; or teach that step (c) comprises intact protein analysis and deconvolution as recited in present claim 26.
However, Elgar teaches that the most common method for analyzing whey proteins is LC, particularly HPLC such as reversed-phase RP-HPLC (page 184, column 1, 2nd paragraph). Elgar teaches that RP-HPLC can be coupled with ESI-MS for a more complete separation of major whey proteins such as proteose peptones with good recovery and suitable for quantitation (abstract; page 184, column 1, 3rd paragraph). Therefore, Elgar discloses step (b) of the claimed method.
It would have been obvious for a person of ordinary skill in the art to have modified the method of Etzel to include subjecting a whey protein fraction to LC-MS analysis as taught by Elgar. Since Etzel teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104], a skilled practitioner would be motivated to consult Elgar to determine a suitable known method of determining and quantifying the proteins in the whey protein fraction of Etzel. In consulting Elgar, the skilled practitioner would readily recognize that RP-HPLC is a known method of quantifying milk proteins including proteose peptones comprising PP8 fast, PP8 slow, and PP-5 and that this known method may be coupled with ESI-MS in order to optimize the quantification process. Therefore, the combination of Etzel and Elgar renders subjecting a whey protein fraction to LC-MS analysis as recited in step (b) of present claim 8 obvious.
The combination of Etzel and Elgar does not teach step (c) of the method as recited in present claim 8; or teach that step (c) comprises intact protein analysis and deconvolution as recited in present claim 26.
However, Vincent teaches that determination and quantification of components by LC and MS are performed by detecting compounds of defined m/z values (corresponding to detecting bCN in the milk samples using the defined m/z values of bCN standards); and deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses (page 12, 2nd paragraph; page 16, Fig. 4, Panels F and H; pages 23-24, section labeled “1.2. Mass spectrometry”). Vincent also teaches that the preparation of milk samples for intact protein analysis has been well established (page 3, 3rd paragraph), thereby disclosing that intact milk protein analysis using LC-MS is well established in the art. Therefore, Vincent discloses step (c) of the claimed method.
It would have been obvious for a person of ordinary skill in the art prior to the effective filing date of the present invention to have modified the method of modified Etzel to include performing step (c) by intact protein analysis and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as taught by Vincent. Since (A) Elgar teaches LC-MS analysis as a method of determining and quantifying proteins (page 184, column 1, 2nd paragraph); and (B) Vincent teaches that LC-MS analysis comprises deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses (page 12, 2nd paragraph; page 16, Fig. 4, Panels F and H; pages 23-24, section labeled “1.2. Mass spectrometry”), a skilled practitioner would readily recognize that the method of modified Etzel comprises deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses as recited in step (c) of present claim 6 and as recited in present claim 25. Furthermore, the practitioner would recognize that the step may further comprise intact protein analysis as recited in step (c) of present claim 6 and as recited in present claim 25 since Vincent discloses that intact protein analysis coupled with LC-MS is known in the art. The combination of Elgar and Vincent yields predictable results as this combination represents the combining of prior art elements according to known methods. MPEP §2143.I.A. Therefore, the combination of prior art renders claims 8 and 26 obvious.
Regarding claim 16, Etzel teaches the invention as described above in claim 8, including reducing the content of the A1 β-casein derived proteose peptone comprises gel filtration of the whey protein fraction (corresponding to ion exchange using gel beads [0035] and optionally, subsequent gel filtration [0102]) of the whey protein fraction.
Regarding claim 17, Etzel teaches the invention as described above in claim 8, including the selected whey fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the content of the A1 β-casein derived proteose peptone in the fraction is at most 5 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Regarding claim 18, Etzel teaches the invention as described above in claim 8, including the selected whey fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the A1 β-casein derived proteose peptone content in the fraction is at most 1 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Regarding claim 19, Etzel teaches the invention as described above in claim 8, including the nutritional composition is an infant formula [0143].
Regarding claim 20, Etzel teaches the invention as described above in claim 6, including the selected whey fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the content of the A1 β-casein derived proteose peptone in the fraction is at most 5 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Regarding claim 21, Etzel teaches the invention as described above in claim 6, including the selected whey fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the A1 β-casein derived proteose peptone content in the fraction is at most 1 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Claims 22-23 are rejected under 35 U.S.C. 103 as being unpatentable over Etzel (US 2009/0068326; previously cited) in view of Elgar (Elgar et al., “Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high performance liquid chromatography on polystyrene-divinylbenzene”, 2000, Journal of Chromatograph A, 878, pages 183-196; previously cited) and Vincent (Vincent et al., “Quantitation and Identification of Intact Major Milk Proteins for High-Throughput LC-ESI-Q-TOP MS Analysis”, 2016, PLoS ONE, 11(10); IDS citation) as evidenced by Yadav (Yadav et al., “Cheese whey: A potential resource to transform into bioprotein, functional/nutritional proteins and bioactive peptides”, 2015, Biotechnology Advances, vol. 33, pages 756-774; previously cited) as applied to claim 6 above, and further in view of Scigelova (Scigelova et al., “Orbitrap Mass Analyzer – Overview and Applications in Proteomics”, 2006, Practical Proteomics Journal, https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/pmic.200600528, pages 16-21; previously cited).
Regarding claims 22 and 23, modified Etzel teaches the invention as described above in claim 6, including the method comprises ESI-MS (Elgar, page 184, column 1, 3rd paragraph). Elgar discloses that the mass spectrometer may be a triple quadrupole spectrometer (page 186, column 2, paragraph under section 2.11).
The prior art does not disclose that the mass spectrometry is a high resolution mass spectrometry performed at a resolution above 100,000 as recited in present claims 22 and 23.
However, Scigelova teaches ESI followed by MS wherein the spectrometer used is an orbitrap analyzer (page 18, Fig. 6). Scigelova teaches that, since the commercial introduction of the orbitrap analyzer, the orbitrap analyzer has become the instrument of choice by those skilled in the art due to its accuracy and high resolution (abstract; page 16, 1st-2nd paragraphs under “Introduction”). Scigelova teaches that the maximum resolution of the orbitrap analyzer is just over 100,000 (page 17, paragraph under “Resolving Power”), which overlaps the resolution recited in present claim 23, and thus qualifies as high resolution mass spectrometry as recited in present claim 22.
It would have been obvious for a person of ordinary skill in the art to have modified the method of modified Etzel to include using the orbitrap analyzer for mass spectrometry as taught by Scigelova. Elgar discloses that the method comprises ESI-MS; discloses a desire for high resolution in its method; and discloses using a triple quadrupole spectrometer (page 184, column 1, 2nd - 3rd paragraphs; page 186, column 2, paragraph under section 2.11). Scigelova discloses ESI followed by MS wherein the spectrometer used is an orbitrap analyzer (page 18, Fig. 6). Therefore, Elgar discloses a comparable base device (i.e., a mass spectrometer for ESI-MS) upon which the claimed invention can be seen as an improvement (i.e., the claimed invention seeks to use a mass spectrometer having a high resolution). Since orbitrap analyzers are known in the art to have high accuracy and high resolution when compared to some other mass spectrometers, a skilled practitioner would have been motivated to apply this known spectrometer to the method comprising ESI-MS of the prior art. The practitioner would have had a reasonable expectation of success since the use of known techniques to improve similar methods in the same way renders the claimed invention obvious. MPEP 2143.I.D.
Response to Arguments
Claim Rejections – 35 U.S.C. §112(b) of claims 6-8 and 16-24: Applicant amended the claims to fully address the rejections. Therefore, the rejections are withdrawn.
Claim Rejections – 35 U.S.C. §103 of claims 6-8, 16-21, and 24 over Etzel, Elgar, and Riggs as evidenced by Yadav and Vincent; claims 22-23 over Etzel, Elgar, Riggs, and Scigelova as evidenced by Yadav and Vincent.
Applicant’s amendments and arguments have been fully considered, and the amendments are considered to overcome the rejections stated in the previous Office Action. However, claims 6-8, 16-21, and 24 now stand rejected by the combination of Etzel, Elgar, and Vincent as evidenced by Yadav while claims 22-23 now stand rejected by the combination of Etzel, Elgar, Vincent, and Scigelova as evidenced by Yadav.
Applicant amended the claim to exclude enzymatic digest by tryptic digest from the claimed list of options for peptide analysis in step (c) of present claims 6 and 8. Applicant argued that neither Etzel nor Elgar disclose step (c) as now recited in the amended claims (Applicant’s Remarks, page 6, 7th paragraph – page 8, 2nd paragraph).
However, as described above in the new grounds of rejection necessitated by the amendment of the claims, the combination of Etzel, Elgar, and Vincent render the claimed step (c) obvious. As described above in the rejections of claims 6 and 8, since (A) Elgar teaches LC-MS analysis as a method of determining and quantifying proteins (page 184, column 1, 2nd paragraph); and (B) Vincent teaches that LC-MS analysis comprises deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses (page 12, 2nd paragraph; page 16, Fig. 4, Panels F and H; pages 23-24, section labeled “1.2. Mass spectrometry”), a skilled practitioner would readily recognize that the method of modified Etzel comprises deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses as recited in step (c) of present claims 6 and 8. Furthermore, the practitioner would recognize that the step may further comprise intact protein analysis as recited in step (c) of present claims 6 and 8 since Vincent discloses that intact protein analysis coupled with LC-MS is known in the art. The combination of Elgar and Vincent yields predictable results as this combination represents the combining of prior art elements according to known methods. MPEP §2143.I.A. Therefore, the combination of prior art renders step (c) of claims 6 and 8 obvious.
Applicant then argued that the cited prior art references do not recognize that A1-derived proteose peptones are present in whey fractions and in A2-based products while the Applicant disclosed that these proteose peptones are reliably detected and quantified in the presently claimed methods. Applicant argued that the present invention enables the selection and/or processing of whey fractions to control the proteose peptone content which was not previously achievable. Applicant argued that the claimed threshold of 10 wt.% or less is not arbitrary but rather a non-obvious part of the Applicant’s technical contribution as the present specification discloses that the reduced proteose peptone content can treat, prevent, and/or ameliorate abdominal pain, and/or lactose intolerance, and improve stool consistency in an infant (Applicant’s Remarks, page 8, 3rd paragraph – page 9, 3rd paragraph).
However, in response to Applicant’s assertion that that the cited prior art references do not recognize that A1-derived proteose peptones are present in whey fractions and in A2-based products while the Applicant disclosed that these proteose peptones are reliably detected and quantified in the presently claimed methods, the fact that the inventor has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious. See Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985).
In response to Applicant’s assertion that the present invention enables the selection and/or processing of whey fractions to control the proteose peptone content, which was not previously achievable, the present claims do not recite any method of processing of whey fractions, but merely state “providing a whey protein fraction”. Therefore, the claims do not require any method of processing of a whey protein fraction, let alone any method of processing of a whey protein fraction disclosed by the Applicant. Furthermore, the claimed method comprises analytical steps which are known in the art (i.e., intact protein analysis, deconvolution, peptide analysis). Therefore, it is not clear as to what Applicant views as being an inventive step recited in the present claims.
In response to Applicant’s assertion that the claimed threshold of 10 wt.% or less is not arbitrary but rather a non-obvious part of the Applicant’s technical contribution as the present specification discloses that the reduced proteose peptone content can treat, prevent, and/or ameliorate abdominal pain, and/or lactose intolerance, and improve stool consistency in an infant, claim 6 and its dependents do not recite a nutritional composition so that any benefits of consuming a composition having the claimed proteose peptone content are not necessarily associated with claim 6 and its dependents. Also, claim 8 and dependent claims 16-18, 20, and 26 do not recite that the composition is for infants. Therefore, the asserted benefits to infants are not necessarily associated with claims 8, 16-18, 20, and 26.
Claim 19 is the only claim which recites that the composition is infant formula. However, neither claims 8 nor 19 recite an amount of proteose peptone in the nutritional composition. Therefore, the composition/infant formula may have an amount of proteose peptone that exceeds 10 wt.%. Furthermore, Applicant has not demonstrated criticality of the claimed amount of proteose peptone; and has not linked the claimed amount of proteose peptone to any of the asserted benefits. Therefore, the claimed amount of proteose peptone amounts to nothing more than an arbitrary selection.
Since the new combination of prior art has been shown to render the present claims obvious and Applicant’s arguments have been shown to be unpersuasive, the rejections of the claims stand as written herein.
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.
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/K.P.K./Examiner, Art Unit 1791
/Nikki H. Dees/Supervisory Patent Examiner, Art Unit 1791
Prosecution Insights