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 .
Status of the Claims
The amendment of 09/05/2025 has been entered (claim set as filed on 09/05/20251). 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.
Withdrawn Objections/Rejections
The rejections of claims 1-2, 5-6, and 11-14 under 35 U.S.C. 103 set forth in the previous Office action are withdrawn in light of the amendment filed on 09/05/2025, which narrowed the scope of base claim 1 and canceled claims 13-14. New rejections have been placed as discussed below.
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 newly rejected as necessitated by amendment 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’, Belhamdi et al. ("A kinetic, equilibrium and thermodynamic study of L-phenylalanine adsorption using activated carbon based on agricultural waste (date stones)", published on 10/01/2016, Journal of Applied Research and Technology, Vol. 14, pages 354-366), hereinafter ‘Belhamdi’, Yongzhi et al. (CN105197926A, published on 12/30/2015), hereinafter ‘Yongzhi’, and 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, pertaining to the method, Etzel teaches a method for producing glycomacropeptide ("process for producing CMP", column 3, lines 5-6) comprising:
(A) bringing a whey protein mixture comprising glycomacropeptide into contact with
activated carbon ("process for producing CMP from whey"; "contacting the fraction
containing CMP with an adsorbent such as ... activated carbon,"; column 3, lines 5-
6; column 8, lines 37-39); and
(B) separating the glycomacropeptide from the activated carbon. Etzel teaches:
" ... 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 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.
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 teaches:" ... 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 32-41) 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 (specification page 11, lines 2-6).
Regarding claims 11 and 12, Etzel teaches wherein the whey protein mixture contains a protein containing phenylalanine residues ("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 1000 ppm by mass to less than 4,955 ppm by mass, in terms of solids (instant claim 1),
wherein separating the glycomacropeptide having a phenylalanine concentration of 1,000 ppm by mass or less, in terms of solid content (instant claims 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 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 comprising 3800, 2200, and 1500 ppm of phenylalanine (“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; see Table 4 in column 12).
Additionally, Ayers teaches: “GMP has a number of potential therapeutic uses as well as having functional properties which make it very useful as an ingredient in food compositions. One important utility is as a nutritional component for use in the diets of persons suffering from phenylketonuria (PKU) Phenylketonurics lack Phe hydroxylase in their metabolic system. Therefore, they are unable to utilise Phe present in foods. This can result in a sufficient accumulation of Phe to cause irreversible mental retardation. In order for GMP to be safe for use in feeding to phenylketonurics the Phe level should be as low as possible.” (column 1, lines 38-43).
Belhamdi' s general disclosure relates to producing low cost activated carbons from date stones that can be used for adsorbing L-phenylalanine (see entire document, including abstract).
Regarding claim 1, pertaining to the contact temperature, Belhamdi teaches wherein adsorption experiments with L-phenylalanine and activated carbon were carried out at 20, 25, 35 and 40 °C, and wherein temperature affected adsorption of L-phenylalanine to activated carbon (“adsorption experiments were performed in … flasks containing a mass of adsorbent mixed with a known volume of L-phenylalanine solution … For the temperature effect, 50 mg of activated carbon was added to 50 mL of L-phenylalanine solutions … the flasks were maintained under constant agitation at various temperatures (20, 25, 35 and 40 °C)”, “temperature has a direct influence on the adsorption of amino acids.”; page 356, paragraph 2; page 358, right column, paragraph 2; see Fig. 6).
Yongzhi’s general disclosure relates to “a method for preparing activated carbon by taking enzymolysis lignin as raw material” (paragraph [0002]).
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 (“the material is washed with …, and then dried at 120°C to obtain the product activated carbon. Its specific surface area is 1480 m <sup> 2 </sup> /g and its total pore volume is 1.26 cm <sup> 3 </sup> /g..”; see Example 10, paragraph [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 further 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).
Additionally, 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 wastes from the pulp industry for producing activated carbon (“In the method of the invention, inorganic salts such as sodium chloride, magnesium chloride and calcium chloride with very low volatility are used as activators, which can greatly avoid the serious environmental pollution problem caused by the easy volatilization of activators during the previous chemical activation process …This is a method with great application prospects, and it also provides a very good application path for the comprehensive utilization of waste resources generated in the chemical processing of plant fiber raw materials.”, “lignin is the main source of serious pollution caused by the pulping industry”; paragraphs [0004], [0021]).
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 (“The adsorption of amino acids such as L-phenylalanine and L-histidine was carried out on a series of mesoporous carbons”; page 582, left column, paragraph 2; see abstract, Table 1, and Figure 4A).
While Etzel does not teach wherein the whey protein mixture has a phenylalanine concentration of from more than 1000 ppm by mass to less than 4,955 ppm by mass, in terms of solids (instant claim 1), and wherein (B) comprises separating glycomacropeptide having a phenylalanine concentration of 1,000 ppm by mass or less, in terms of solid content (instant claim 1), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of producing glycomacropeptide, as taught by Etzel, with Ayers’ teachings on phenylalanine concentrations in crude glycomacropeptide and the need for phenylalanine levels being as low as possible, in order to produce a high purity glycomacropeptide product from a crude glycomacropeptide product having a phenylalanine concentration of from 1500 to 3800 ppm by mass, in terms of solids, wherein the purified glycomacropeptide product is essentially free of phenylalanine impurities and therefore contains a phenylalanine concentration of 1,000 ppm by mass or less (in terms of solid content). One would have been motivated to do so, in order to develop a superior glycomacropeptide product that 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 the prior art references to have arrived at the claimed invention because both references are directed at glycomacropeptide, and because Etzel teaches that phenylalanine containing peptide and protein contaminants adsorb to activated carbon (column 8, lines 25-37).
While modified Etzel does not teach 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), 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’s method with Belhamdi’s teachings on temperature effect of L-phenylalanine adsorption to activated carbon, to have developed a method wherein a temperature of the whey protein mixture during the contact with activated carbon in (A) is from 20 °C to 40 °C. One would have been motivated to do so in order to optimize the adsorption of phenylalanine to a specific activated carbon. A skilled artisan would have reasonably expected success in the combination of modified Etzel’s and Belhamdi’s teachings since both references are directed to the adsorption of phenylalanine to activated carbon.
While modified Etzel does not teach 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 1523 m2/g (instant claim 1), wherein said activated carbon is derived from a plant-based carbonaceous material (instant claims 5 and 6), 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 modified Etzel’s method with the lignin derived mesoporous activated carbon taught by Yongzhi and with Goscianska’s teachings on phenylalanine adsorption to mesoporous materials, in order to develop a method for producing glycomacropeptide comprising lignin derived activated carbon wherein the activated carbon comprises a pore volume of 1.26 mL/g, an average pore diameter of 3.4 nm, and a specific surface area of 1,480 m2/g. One would have been motivated to do so in order to develop an improved method for purifying glycomacropeptide that maximizes the removal of phenylalanine and comprises activated carbon that can be produced from waste resources in an environmentally friendly way (Yongzhi, paragraphs [0004], [0021]). A skilled artisan would have reasonably expected success in the combining modified Etzel’s, Yongzi’s and Goscianska’s teachings since all references are directed to porous materials.
Response to Arguments
Applicant has traversed the previous rejection of claims 1-2, 5-6, and 11-14 under 35 U.S.C. 103 as being unpatentable over Etzel, Ayers, Belhamdi, Yongzhi and Goscianska, (remarks, pages 4-6). As discussed above, all rejections have been withdrawn and new rejections presented due to Applicant’s amendment of 09/05/2025. Applicant's arguments filed 09/05/2025 have been fully considered but they are not persuasive.
In Applicant’s reply, Applicant states: “[T]he method of the present application
provides unexpected improvements over the use of cation exchange resins as per Etzel and Ayers. The present application discusses the disadvantages of the use of ion exchange resins in paragraph [0002]. Specifically, with ion exchange resins, elution is performed using salt solutions (often containing high concentrations of salts), leading to salt contamination in the eluted glycomacropeptide solution. Since salts affect food flavor, a high salt concentration is undesirable” (remarks, page 5).
The Examiner responds that the feature reduced salt concentration upon which Applicant relies as unexpected improvement is not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Applicant describes “the combination of Etzel and Ayers does not enable
one of ordinary skill in the art to practice the method described in the present claims without undue experimentation. While Ayers may provide motivation for decreasing phenylalanine level, Ayers does not enable one of ordinary skill in the art to produce a glycomacropeptide having 1000 ppm of phenylalanine, a level significantly lower than the minimum level of 1500 pm taught in Ayers.” (remarks, page 4).
The Examiner responds that the combination of Etzel’s, Ayer’s, Belhamdi’s, Yongzhi’s and Goscianska’s teachings would implicitly result in a glycomacropeptide preparation with the same or similar phenylalanine concentration as claimed. Since Etzel’s teachings provide a method using activated carbon to remove phenylalanine, Ayers provides glycomacropeptide compositions comprising 3800, 2200, and 1500 ppm phenylalanine and motivation to provide a glycomacropeptide essentially free of phenylalanine, Belhamdi’s teachings provide adsorption of phenylalanine to activated carbon at 20-40 °C, Yongzhi’s teachings provide lignin derived 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, it is highly expected that the method taught by Etzel, in view of Ayers, Belhamdi, Yongzhi and Goscianska, would result in a glycomacropeptide with the same or similar phenylalanine concentration as described in claim 1.
Conclusion
No claims are allowed.
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.
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