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 in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 06/12/2026 has been entered.
Claim Status
The amendment of 05/15/2026 has been entered (claim set as filed on 05/15/2026). Claims 1-2, 5-6, and 11-12 are pending in this US patent application. Claims 1-2, 5-6, and 11-12 are currently under examination and were examined on their merits.
Claim Rejections - 35 USC § 112 (b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-2, 5-6, and 11-12 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites ‘the method is free of elution with a salt solution' which is indefinite since it is unclear if ‘free of elution with a salt solution’ means that an elution is not required if a salt solution is used, or if it means free of a salt solution based elution, or it is a negative proviso that allows for elution unless it is an elution with a salt solution . One of ordinary skill in the art would not be able to determine the metes and bounds of the claim, and thus, could not clearly determine how to avoid infringement of claim 1. In the interest of compact prosecution, claim 1 is interpreted to the broadest embodiment claimed.
Claims 2, 5-6, and 11-12, are rejected since they do not clarify the indefinite language of claim 1.
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.
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 factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
Determining the scope and contents of the prior art.
Ascertaining the differences between the prior art and the claims at issue.
Resolving the level of ordinary skill in the pertinent art.
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 1-2, 5-6, and 11-12 are rejected under 35 U.S.C. 103 as being unpatentable over Etzel (US 5968586 A, published on 10/19/1999), hereinafter ‘Etzel’, in view of Ayers et al. (US 6,555,659 B1, published on 04/29/2003), hereinafter ‘Ayers’, in view of Yongzhi et al. (CN105197926A, published on 12/30/2015), hereinafter ‘Yongzhi’, and in view of Goscianska et al. (“Comparison of ordered mesoporous materials sorption properties towards amino acids”, published on 02/02/2013, Adsorption (2013), Vol. 19, pages 581–588), hereinafter ‘Goscianska’.
Etzel' s general disclosure relates to a process for producing CMP from whey comprising fractionating the whey (column 2, lines 57-58). Etzel teaches K-casein macropeptide (CMP) exists as fully-glycosylated CMP (called K-casein glycomacropeptide, or GMP) or nonglycosylated CMP, and that for the purpose of Etzel's invention, all forms of CMP are included (see entire document including column 1, lines 28-35).
Regarding claim 1, please note the rejection under Claim Rejections - 35 USC § 112 (b) above.
Pertaining to the method, Etzel teaches a method for producing glycomacropeptide (column 8, lines 25-41) comprising:
(A) bringing a whey protein mixture comprising glycomacropeptide into contact with
activated carbon ("contacting the fraction containing CMP with an adsorbent such as ... activated carbon"; column 8, lines 25-29 and lines 37-39); and
(B) separating the glycomacropeptide from the activated carbon. Etzel teaches that
“by contacting the fraction containing CMP with an adsorbent such as hydrophobic interaction matrices and activated carbon, peptide and protein contaminants can be removed by adsorption, enriching the fraction in CMP" (column 8, lines 32-41). Since the glycomacropeptide does not adsorb to the activated carbon, and Etzel further teaches that the purified glycomacropeptide is converted into a food product ("the purified CMP may be hydrolyzed to form a food product"; column 8, lines 57-58), it is inherently taught by Etzel' s disclosure that the enriched fraction of glycomacropeptide is separated from the activated carbon.
Pertaining to the method being free of elution with a salt solution, Etzel is silent on using elution to perform the claimed method steps (A) and (B). As such, Etzel’s method using activated carbon to remove phenylalanine from a whey protein mixture is considered free of elution with a salt solution.
Regarding claim 2, Etzel teaches wherein the protein mixture is crude
glycomacropeptide derived from whey ("The fraction containing CMP thus obtained is
substantially free of impurities, but may be further purified by contacting the fraction with one or more adsorbents to remove residual peptide or protein contaminants. The adsorbent or adsorbents may consist of activated carbon"; column 8, lines 25-29).
Etzel discloses: "Hydrophobic interaction matrices such as […] activated carbon may be used to adsorb peptide and protein contaminants containing hydrophobic amino acids such as phenylalanine, tryptophan, and tyrosine. Other whey proteins and peptide hydrolysis products of caseins and whey proteins contain these amino acids whereas CMP does not. Therefore, by contacting the fraction containing CMP with an adsorbent such as hydrophobic interaction matrices and activated carbon, peptide and protein contaminants can be removed by adsorption, enriching the fraction in CMP" (column 8, lines 30-41).
As such, the "fraction containing CMP" that Etzel contacts with activated carbon is a "crudely purified glycomacropeptide containing a phenylalanine component as an impurity that is obtained from whey by industrial separation and purification”, thus satisfying the definition of the term "crude glycomacropeptide derived from whey" as recited in the instant specification (page 11, lines 2-6).
Regarding claims 11 and 12, Etzel teaches wherein the whey protein mixture comprises a protein containing a phenylalanine residue ("The fraction containing CMP thus obtained is substantially free of impurities, but may be further purified by contacting the fraction with one or more adsorbents to remove residual peptide or protein contaminants. The adsorbent or adsorbents may consist of activated carbon", "activated carbon may be used to adsorb peptide and protein contaminants containing hydrophobic amino acids such as phenylalanine”, “Other whey proteins and peptide hydrolysis products of caseins and whey proteins contain these amino acids whereas CMP does not"; column 8, lines 25-37).
Etzel does not teach
wherein the whey protein mixture has a phenylalanine concentration of from more than 1,000 ppm by mass to less than 4,955 ppm by mass, in terms of solids (instant claim 1),
wherein the separated glycomacropeptide has a phenylalanine concentration of 1,000 ppm by mass or less, in terms of solid content (instant claim 1).
wherein a temperature of the whey protein mixture during the contact with activated carbon in (A) is from 20 °C to 80 °C (instant claim 1),
wherein a pore volume of the activated carbon is at least 0.65 mL/g, an average pore diameter of the activated carbon is at least 2.1 nm, and a specific surface area of the activated carbon is from 1,289 m2/g to 1,523 m2/g (instant claim 1),
wherein a ratio of a phenylalanine concentration in the glycomacropeptide to a phenylalanine concentration in the whey protein mixture is 0.7 or less (instant claim 1).
wherein the activated carbon is derived from a plant-based carbonaceous material (instant claims 5-6),
Ayers’ general disclosure relates to “a method for the purification of glycomacropeptide (GMP) with an amino acid composition containing no greater that 0.5% (w/w) phenylalanine” (see entire document, including abstract).
Regarding claim 1, pertaining to the phenylalanine concentration in a whey protein mixture, Ayers teaches glycomacropeptide preparations derived from whey having a phenylalanine concentration of 3,800, 2,200, and 1,500 ppm (“isolation of GMP to a purity under which it has an amino acid composition containing less than 0.5% w/w of phenylalanine (Phe )”, “Purity and Yield of GMP … Phe 0.38 %, 0.22 %, and 0.15 %”; column 1, lines 14-16; column 11, lines 29-31; see Example 8 in column 12, lines 63-67 and column 13, lines 1-18; see Table 4 in column 12). Ayer’s glycomacropeptide preparations are considered “crude glycomacropeptide”.
Additionally, Ayers teaches that “[i]n order for GMP to be safe for use in feeding to phenylketonurics the Phe level should be as low as possible” (column 1, lines 41-44).
Yongzhi’s general disclosure relates to “a method for preparing activated carbon by taking enzymolysis lignin as raw material” (paragraph [0002]; see abstract). Yongzhi teaches wherein the method for producing activated carbon derived from enzymatic lignin employs activators with low volatility which reduces environmental pollution, and further uses lignin waste for producing activated carbon (paragraphs [0004], [0021]; see abstract).
Regarding claim 1, pertaining to the activated carbon, Yongzhi teaches an activated carbon wherein the pore volume of the activated carbon is 1.26 mL/g, and the specific surface area of the activated carbon is 1480 m2/g (see Example 10, paragraphs [0042] - [0043]). The average pore diameter of the activated carbon taught by Yongzhi is 3.4 nm, as calculated by the formula cited in the instant specification (“the average pore diameter of the activated carbon may be determined by an expression: 4000 x [pore volume (mL/g) described above/specific surface area (m2/g) described below].”; see instant specification page 16, lines 21-24). It is noted that the instant specification discloses that ‘pore volume’ corresponds to ‘total pore volume’ (“The pore volume (total pore volume) of the activated carbon”; see page 15, line 31).
Regarding claims 5 and 6, pertaining to the activated carbon, Yongzhi teaches wherein the activated carbon is derived from the plant-based carbonaceous material lignin (see abstract and Example 10, paragraphs [0042] - [0043]).
Goscianska’s general disclosure relates to the adsorption of amino acids such as L-phenylalanine and L-histidine to a series of mesoporous carbons (see entire document, including abstract).
Regarding claim 1, pertaining to the pore size, Goscianska teaches “great potential of mesoporous materials as proper adsorbents of amino acids” (page 582, left column, paragraph 2), and wherein phenylalanine adsorbs to the mesoporous materials CKIT-6 , CSBA-16 , CSBA-15 having average pore diameters of 4.13, 3.62, and 3.29 nm, respectively, and pore volumes of 1.02, 0.98, and 0.97 mL/g, respectively (page 582, left column, paragraph 2; see abstract, Table 1, and Figure 4A).
Pertaining to the contact temperature in (A), Goscianska teaches determining adsorption of amino acids including phenylalanine at 20 °C (page 584, right column, paragraph 1 - page 585, left column, paragraph 1).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of Etzel and Ayers and utilize a whey protein mixture that has a phenylalanine concentration of from more than 1000 ppm by mass to less than 4,955 ppm for separating the glycomacropeptide having a phenylalanine concentration of 1000 ppm by mass or less. One would have been motivated to do so to prepare a glycomacropeptide product that is essentially free of phenylalanine impurities and is suitable as a dietary source of amino acids for patients suffering from phenylketonuria (Ayers, column 1, lines 38-43). A skilled artisan would have had a reasonable expectation of success in combining Etzel’s and Ayers’ teachings because both references are directed to preparing glycomacropeptide, and because Etzel teaches that phenylalanine containing peptide and protein contaminants adsorb to activated carbon (column 8, lines 25-37).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have combined Etzel, Ayers, Yongzhi , and Goscianska’s and utilize the claimed carbon and temperature. One would have been motivated to do so to obtain a method for purifying glycomacropeptide that maximizes the removal of phenylalanine and comprises activated carbon that can be produced from lignin waste in an environmentally friendly way (Yongzhi, paragraphs [0004], [0021]; see abstract). A skilled artisan would have reasonably expected success since Etzel’s method utilizes activated carbon in the process.
One would have been further motivated to utilize the instant temperature since Goscianska’s teaches the instant temperature for proper phenylalanine adsorption to porous materials.
Regarding the phenylalanine concentration in the separated glycomacropeptide in instant claim 1 (B), and regarding the ratio of a phenylalanine concentration in the glycomacropeptide to a phenylalanine concentration in the whey protein mixture in instant claim 1, since Etzel teaches a method using activated carbon to remove phenylalanine from crude glycomacropeptide without salt elution, Ayers discloses crude glycomacropeptide comprising 3800, 2200, and 1500 ppm phenylalanine, Yongzhi provides a mesoporous activated carbon with a pore volume of 1.26 mL/g, a specific surface area of 1480 m2/g, and a pore diameter of 3.4 nm, and Goscianska’s teaches phenylalanine adsorption to mesoporous materials and an adsorption temperature of 20 °C, it is highly likely that the method taught by Etzel in view of Ayers, Yongzhi and Goscianska, would result in a glycomacropeptide having the same or similar phenylalanine concentration, and would result in the same or similar ratio of a phenylalanine concentration in the glycomacropeptide to a phenylalanine concentration in the whey protein mixture as described in instant claim 1.
Response to Arguments
Applicant has traversed the previous rejection of claims 1-2, 5-6, and 11-12 under 35 U.S.C. 103 as being unpatentable over Etzel, Ayers, Belhamdi, Yonghzi, and Goscianska in the reply filed on 05/15/2026 (remarks, pages 4-5). Belhamdi is no longer relied upon in the above rejection. Applicant's arguments regarding Etzel’s and Ayers’ teachings have been fully considered but they are not persuasive.
In Applicant’s reply, Applicant states that both “Etzel and Ayers require the use of an elution step”, and that “the cited references, alone and in combination, do not enable one of ordinary skill in the art to produce a glycomacropeptide that adheres to the claims without as salt-based elution” (remarks, page 4).
The Examiner notes the rejection under Claim Rejections - 35 USC § 112 (b) above, and responds that, as discussed above under Claim Rejections - 35 USC § 103, Etzel teaches a method using activated carbon to remove phenylalanine from a crude glycomacropeptide wherein the method does not require an elution step (Etzel, column 8, lines 32-41). The Examiner notes that the instant specification describes wherein “crude glycomacropeptide derived from whey may be used as the whey protein mixture” (page 10, line 30 -page 11, line 2). It appears Applicant’s arguments regarding an elution step are directed to Etzel’s teachings on preparing crude glycomacropeptide which involves ion exchange chromatography which may comprise an elution step using a salt solution (Etzel, column 7, lines 23-28; see claim 1). However, these method steps are not part of Etzel’s method to remove phenylalanine from crude glycomacropeptide using activated carbon. It is noted that the instant specification discloses that “when crude glycomacropeptide derived from whey is used as the whey protein mixture, crude glycomacropeptide obtained at any stage in a process of industrially separating and purifying glycomacropeptide from whey may be used” (lines 23-27). The specification further cites ion exchange chromatography as a method for obtaining crude glycomacropeptide (page 11, lines 11-12).
Pertaining to Applicant’s arguments regarding Ayers, Ayers’ teachings are relied upon for disclosing crude glycomacropeptide comprising 3800, 2200, and 1500 ppm phenylalanine, and for providing motivation to prepare a glycomacropeptide essentially free of phenylalanine.
Applicant describes that “none of the cited references teaches a method in which a ratio of a phenylalanine concentration in the glycomacropeptide to a phenylalanine concentration in the whey protein mixture is 0.7 or less”, and that “the references do not teach any phenylalanine concentration of the whey protein mixture or any ratio of the phenylalanine concentration of the whey protein mixture and glycomacropeptide” (remarks, page 5).
The Examiner responds that, as discussed above under Claim Rejections - 35 USC § 103, Ayers teaches a whey protein mixture (crude glycomacropeptide) comprising 3800, 2200, and 1500 ppm phenylalanine corresponding to the recited range in instant claim 1 (A).
Pertaining to the phenylalanine concentration in the separated glycomacropeptide (B), and to the ratio of a phenylalanine concentration in the glycomacropeptide to a phenylalanine concentration in the whey protein mixture in instant claim 1, the recited phenylalanine concentration and ratio would naturally result from performing the method according to instant claim 1, as discussed above under Claim Rejections - 35 USC § 103. Since Etzel in view of Ayers, Yongzhi and Goscianska teaches the claimed method of claim 1, it is highly likely that the method taught by modified Etzel would result in a glycomacropeptide having the same or similar phenylalanine concentration, and would further result in the same or similar ratio of a phenylalanine concentration in the glycomacropeptide to a phenylalanine concentration in the whey protein mixture as described in claim 1. If Applicant’s method requires additional features to obtain the recited phenylalanine concentration (B) and ratio recited in instant claim 1, these features have not been claimed.
Conclusion
No claims are allowed.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SANDRA ZINGARELLI whose telephone number is (703)756-1799. The examiner can normally be reached M-F 9-5.
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/SANDRA ZINGARELLI/Examiner, Art Unit 1653
/SHARMILA G LANDAU/ Supervisory Patent Examiner, Art Unit 1653
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