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 Request for Continued Examination (RCE under 37 CFR 1.114), the Response, and Amendment filed 01/16/2026 is acknowledged.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 7, 9-13, 16-38
Withdrawn claims: None
Previously cancelled claims: 1-6, 8, 15
Newly cancelled claims: None
Amended claims: 7
New claims: 38
Claims currently under consideration: 7, 9-13, 16-38
Currently rejected claims: 7, 9-13, 16-38
Allowed claims: None
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 01/16/2026 has been entered.
Claim Objections
Claim 7 is objected to because “glycated by incubating with 55-65% of a reducing sugar” should be read as “glycated by incubating the enzyme with 55-65% of a reducing sugar”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 7, 9-13, and 16-38 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 77 recites that the enzyme is “glycated by incubating at 55-65% of a reducing sugar for 60-80 hours at a temperature of 50°C-65°C”. However, neither the previous versions of the claims nor the present specification discloses such conditions for any other sugar besides glucose so that this amendment broadens the conditions to cover sugars besides glucose. Therefore, the amendment constitutes new matter.
Claims 9-13 and 16-38 are rejected by reason of dependency from claim 7.
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.
Claims 7, 9-13, and 16-38 are rejected under 35 U.S.C. 112(b) 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 7 recites “55-65% of a reducing sugar”, but does not recite any unit of measurement associated with the percentage (e.g., wt.%, vol.,%). Therefore, the claim is indefinite.
For the purpose of this examination, the percentage will be interpreted as being a weight percentage.
Claim 7 also recites a step (f) of combining the milk powder and the glycated enzyme at a temperature of 50-60°C to increase the amount of GOS in the milk powder compared to the amount of GOS formed by combining the milk powder and glycated enzyme at a temperature of 5°C. Since this step is labeled as step (f); and this step recites “milk powder”, it seems as if this step is to be performed after step (e). However, the milk substrate and the glycated enzyme were already combined in step (b) to form the milk powder of step (e). Therefore, it is not clear where step (f) is meant to occur. As such the claim is indefinite.
For the purpose of this examination, step (f) will be interpreted as meaning that step (b) further comprises combining the milk substrate and the glycated enzyme at a temperature of 50-60°C so that the milk powder produced in step (e) has an increased amount of GOS compared to a milk powder produced by combining the milk substrate and the glycated enzyme at a temperature of 5°C.
Claims 9-13 and 16-38 are rejected by reason of dependency from claim 7.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 7, 10-13, 16-22, and 25-37 are rejected under 35 U.S.C. 103 as being unpatentable over Silver (US 2009/0297660; previously cited) in view of Deya (EP0458358; IDS citation), Larsen (US 2015/0223481; previously cited), and Liu (Liu et al., “Glycation a promising method for food protein modification: Physicochemical properties and structure, a review”, 2012, Food Research International, vol. 49, pages 170-183) as evidenced by search results filed 05/13/2021.
Regarding claims 7, 31, and 32, Silver teaches a method for producing a milk product (corresponding to dairy substrate that has been treated with enzymes, but has not been processed to form a cheese product (Fig. 1, [0025])), wherein the method consists of: (a) providing a milk substrate comprising at least 7 wt.% lactose, such as about 20 wt.% to about 50 wt.% [0024], which overlaps the claimed content range; (b) contacting a milk substrate with an enzyme having transgalactosylating activity [0091] for 2-24 hours [0089], which falls within the claimed time range, at a temperature of about 40°C to about 65°C [0092], which encompasses the claimed temperature range; (c) inactivating the enzyme [0096]; and (d) thereby obtaining a milk product from a dairy substrate wherein about 25-100% of the lactose present in the dairy substrate is converted and 50-75 wt.% of the in situ produced sugars in the milk product are DP3+ GOS [0025], which falls within the claimed relative concentration range for DP3+ GOS; and wherein at least about 0.875 wt.% of the milk product is in situ produced DP3+ GOS (corresponding to a dairy substrate comprising a minimum of 7 wt.% lactose wherein a minimum of about 25% of the lactose is converted and wherein a minimum of 50 wt.% of those in situ produced sugars are DP3+ GOS), which overlaps the claimed concentration of in situ produced DP3+ GOS in the milk product.
In regards to the encompassing ranges and overlapping ranges, 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. Therefore, the selection of values within the encompassing and overlapping ranges renders the claimed enzyme treatment temperature recited in step (f) of the present method, the claimed lactose concentration, and the claimed concentration of in situ produced DP3+ GOS in the milk product obvious.
Silver also teaches that the milk substrate is reconstituted milk powder (corresponding to rehydrated powder) or concentrated milk [0086]. Silver teaches that the enzyme-treated milk product of step (d) is dehydrated prior to it being processed into cheese [0083]. Silver does not teach that the enzyme-treated milk product is dried to obtain a milk powder product as recited in step (e). Silver also does not teach that the enzyme having transgalactosylating activity: (1) was glycated according the method recited in lines 6-8 of present claim 7; (2) has the features recited in lines 14-17 of present claim 7; or (3) the lengths recited in present claims 31 and 32.
However, Deya teaches a milk powder product having a high galacto-oligosaccharide content produced by treating concentrated milk with β-galactosidase (page 3, lines 4-9, 16-19) and spray drying the treated milk as in ordinary spray drying for skim milk (page 4, lines 12-13).
It would have been obvious for a person of ordinary skill in the art to have modified the method of Silver to include drying the enzyme-treated milk product of step (d) into a powder as taught by Deya. Since Silver teaches that the treated milk product is dehydrated [0083], but does not disclose a method of dehydrating the powder, a skilled practitioner would have been motivated to consult an additional reference such as Deya in order to determine a suitable method of dehydrating an enzyme-treated milk product; therefore, the claimed step (e) and the claimed milk powder product is rendered obvious.
The combination of Silver and Deya teaches an enzyme-treated milk product (Silver, Fig. 1, [0025]) which was spray dried into a powder (Deya, page 4, lines 12-13), wherein about 25-100% of the lactose present in the dairy substrate is converted and 50-75 wt.% of the in situ produced sugars in the milk product are DP3+ GOS (Silver [0025]); and wherein at least about 0.875 wt.% of the milk product is in situ produced DP3+ GOS. The combination of Silver and Deya also teaches that the enzyme treatment step may occur at a temperature of about 40°C to about 65°C (Silver [0092]). Therefore, the combination of Silver and Deya at least suggests that the milk powder produced in step (e) has an increased amount of GOS compared to a milk powder produced by combining the milk substrate and the glycated enzyme at a temperature of 5°C so that the method of the prior art is a method for increasing an amount of GOS in a milk powder as recited in present claim 7. Further, the Office does not have laboratory facilities to test claim limitations drawn toward results of practicing the method as claimed. Accordingly, such an increase in GOS produced by the enzyme treatment at 50-60°C in comparison to GOS produced by enzyme treatment at 5°C does not serve to distinguish the method as claimed from the prior art and is thus considered obvious to one having ordinary skill in the art, especially in light of the prior art teaching enzyme treatment at temperatures encompassing 50-60°C.
Silver teaches that the enzyme used to treat the milk has transgalactosylation activity and may be produced from cell cultures of Bifidobacterium infantis [0090]-[0091]. The combination of Silver and Deya does not teach that the enzyme having transgalactosylating activity: (1) was glycated according the method recited in lines 6-8 of present claim 7; (2) has the features recited in lines 14-17 of present claim 7; or (3) the lengths recited in present claims 31 and 32.
However, Larsen teaches a spray-dried [0010], enzyme-treated dairy product (corresponding to a dairy product comprising GOS formed in situ by trans-galactosylating β-galactosidase) [0171-[0172], [0239] is manufactured by any method known in the art [0177]. Larsen teaches that the enzymes used to treat the dairy product are GOS-producing enzymes [0010] produced from Bifidobacterium infantis [0309]. Larsen also teaches that the enzyme contains a fragment of SEQ ID NO:22 truncated from the C-terminal end of the enzyme [0026], [0119] to be a length of at least 900 amino acid residues [0208]. Amino acids 1-1304 of the enzyme having SEQ ID NO:22 disclosed in Larsen is 99.7% identical to amino acids 1-1304 of the claimed enzyme having SEQ ID NO: 1 as evidenced by the search results filed 05/13/2021 (Result No. 15 in the database labeled “Published_Applications_AA_Main”). Since amino acids 1-1304 of the enzyme having SEQ ID NO:22 disclosed in Larsen is nearly 100% identical to amino acids 1-1304 of the claimed enzyme having SEQ ID NO: 1, truncated versions of SEQ ID NO: 22 would have a range of lengths that overlap the lengths of 900-1350 amino acids, 1300-1305 amino acids, and 1302 or 1304 amino acids recited in present claims 7, 31, and 32.
It would have been obvious for a person of ordinary skill in the art to have modified the method of Silver to include using an enzyme containing a fragment of SEQ ID NO:22 truncated from the C-terminal end of the enzyme disclosed as taught by Larsen. Since Silver discloses that the enzyme used to treat the milk has transgalactosylation activity and may be produced from cell cultures of Bifidobacterium infantis [0090]-[0091], but does not specify such an enzyme, a skilled practitioner would have been motivated to consult an additional reference such as Larsen in order to determine a suitable enzyme, thereby rendering the claimed enzyme identity and lengths recited in present claims 7, 31, and 32 obvious.
Modified Silver discloses that the transgalactosylating enzyme may be stabilized in accordance with methods known in the art (Larsen [0262]). The prior art does not teach that the enzyme having transgalactosylating activity: (1) was glycated according the method recited in lines 6-8 of present claim 7; or (2) has been modified by glycation in at least one lysine and/or arginine residue of the enzyme as recited in lines 16-17 of present claim 7.
However, Liu teaches that glycation is known as being an effective method for improving the functional properties of food proteins such as heat stability; and that glycoprotein conjugates formed by glycation, also known as the Maillard reaction, has received much attention in recent years (page 171, 1st column, 2nd paragraph; page 172, 1st column, 2nd paragraph under section 2.2). Liu teaches that glycation most often uses the lysine residue as the primary source of reactive amino groups; and that glycation uses arginine residues as reactive amino groups to a lesser extent (page 172, 1st column, 1st paragraph under section 2.2). Liu also teaches that the reaction factors such as temperature, time, and amino group to reducing sugar ratio influence the yields and type of glycation products (page 172, 1st column, 2nd paragraph). Liu discloses that a temperature such as 60°C, a ratio of amino group to reducing sugar of 1:1, and a time of 72 hours may be used in a glycation reaction of a protein and a reducing sugar (page 173, Table 1, 6th reference in Table).
It would have been obvious for a person of ordinary skill in the art to have modified the enzyme having transgalactosylating activity of modified Silver by glycation of at least one lysine residue or arginine residue as taught by Liu. Since modified Silver discloses that the transgalactosylating enzyme may be stabilized in accordance with methods known in the art (Larsen [0262]), but does not disclose any specific method of stabilizing the enzyme, a skilled practitioner would have been motivated to consult an additional reference such as Liu in order to determine a suitable method of stabilizing the enzyme, thereby rendering the claimed modification by glycation in at least one lysine residue and/or arginine residue of the enzyme as recited in lines 16-17 of present claim 7 obvious.
In regard to glycating the enzyme according the method recited in lines 6-8 of present claim 7, as the yields and type of glycation products are variables that can be modified, among others, by adjusting reaction factors such as temperature, time, and amino group to reducing sugar ratio, the claimed temperature, time, and amount of reducing sugar would have been considered a result effective variable by one having ordinary skill in the art before the effective filing date of the invention. As such, without showing unexpected results, the claimed temperature, time, and amount of reducing sugar cannot be considered critical. Accordingly, one of ordinary skill in the art before the effective filing date of the invention would have optimized, by routine experimentation, the claimed temperature, time, and amount of reducing sugar in the glycation process by using a temperature of 60°C, a ratio of amino group to reducing sugar of 1:1, and a time of 72 hours as a guide to obtain the desired glycation products as taught by Liu (In re Boesch, 617 F.2d. 272, 205 USPQ 215 (CCPA 1980)), since it has been held that where the general conditions of the claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. (In re Aller, 105 USPQ 223). “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” See In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). The discovery of an optimum value of a known result effective variable, without producing any new or unexpected results, is within the ambit of a person of ordinary skill in the art. See In re Boesch, 205 USPQ 215 (CCPA 1980). MPEP § 2144.05.II.
Regarding claim 10, Silver teaches the invention as described above in claim 7, including the milk substrate does not comprise added lactose (corresponding to the milk substrate being powdered or concentrated liquid dairy ingredients replacing all of the conventional starting materials) [0086].
Regarding claim 11, modified Silver teaches the invention as described above in claim 7, including the milk substrate comprises 20-50 wt.% dry matter (Deya, page 3, lines 16-18), which overlaps the claimed concentration. A selection of a value within the overlapping range renders the claimed concentration obvious. MPEP 2144.05.I.
Regarding claim 12, Silver teaches the invention as described above in claim 7, including 50-75 wt.% of the total free carbohydrates in the milk product is in situ produced DP3+ GOS [0025]; therefore, 50-75 wt.% of the total free carbohydrates in the milk product are in situ produced DP2+ GOS, which falls within the claimed relative concentration range.
Regarding claim 13, Silver teaches the invention as disclosed above in claim 7, including the enzyme having transgalactosylating activity is a beta-galactosidase [0092] having a ratio of transgalactosylating to hydrolyzing activity above about 0.3 [0091], which overlaps the claimed ratio. Silver does not teach measuring enzyme activity in a 60% solution of skim milk powder after 24 hours at 50°C using an enzyme concentration of 13 LAU(C) per g lactose, but the Office does not have laboratory facilities to measure transgalactosylating activity or hydrolyzing activity. Accordingly, such a method of determining transgalactosylating to hydrolyzing activity does not serve to distinguish the invention as claimed from the prior art and is thus considered obvious to one having ordinary skill in the art.
Regarding claims 16, 17, 18, and 19, Silver teaches the invention as described above in claim 7, including 50-75 wt.% of the total free carbohydrates in the milk product is in situ produced DP3+ GOS [0025], which overlaps the claimed relative concentrations recited in present claims 16. 17. 18, and 19. The selection of a value within the overlapping ranges renders the claimed ranges obvious. MPEP 2144.05.I.
Regarding claim 20, Silver teaches the invention as described above in claim 7, including the milk substrate is reconstituted skim milk powder or condensed milk (corresponding to concentrated liquid dairy products) [0086].
Regarding claims 21 and 22, Silver teaches the invention as described above in claim 7, including the milk substrate comprises 20-50 wt.% dry matter (Deya, page 3, lines 16-18), which overlaps the claimed concentrations. A selection of a value within the overlapping ranges renders the claimed concentrations recited in present claims 21 and 22 obvious. MPEP 2144.05.I.
Regarding claims 25, 26,and 27, Silver teaches the invention as described above in claim 7, including 50-75 wt.% of the total free carbohydrates in the milk product is in situ produced DP3+ GOS [0025]; therefore, 50-75 wt.% of the total free carbohydrates in the milk product are in situ produced DP2+ GOS, which falls within the claimed relative concentration range recited in present claim 25 and overlaps the claimed relative concentration range recited in present claims 26 and 27. MPEP 2144.05.I.
Regarding claims 28, 29, and 30, Silver teaches the invention as disclosed above in claim 13, including the enzyme having transgalactosylating activity is a beta-galactosidase [0092] having a ratio of transgalactosylating to hydrolyzing activity above about 0.3 [0091], which encompasses the claimed ratios recited in present claims 28, 29, and 30. The selection of a value within the encompassing ranges renders the claimed ratios obvious. MPEP 2144.05.I.
Regarding claim 33, Silver teaches the invention as described above in claim 7, including about 25-100% of the lactose present in the dairy substrate is converted and 50-75 wt.% of the in situ produced sugars in the milk product are DP3+ GOS [0025], which falls within the claimed relative concentration range for DP3+ GOS; and wherein at least about 0.875 wt.% of the milk product is in situ produced DP3+ GOS (corresponding to a dairy substrate comprising a minimum of 7 wt.% lactose wherein a minimum of about 25% of the lactose is converted and wherein a minimum of 50 wt.% of those in situ produced sugars are DP3+ GOS), which encompasses the claimed concentration of in situ produced DP3+ GOS in the milk product. The selection of a value within the encompassing range renders the claimed concentration obvious. MPEP 2144.05.I.
Regarding claims 34 and 35, Silver teaches the invention as described above in claim 7, including the milk substrate comprises least 7 wt.% lactose [0024] and that about 25-100% of the lactose present in the dairy substrate is converted to GOS to form the milk product [0025]. Therefore, the milk product comprises amounts of lactose as low as 0 wt.% (corresponding to 100% of the lactose in the milk substrate being converted), thereby providing a range of lactose concentrations that overlaps the concentrations recited in present claims 34 and 35. The selection of a value within the overlapping ranges renders the claims obvious. MPEP 2144.05.I.
Regarding claim 36, modified Silver teaches the invention as described above in claim 7, including the drying of step (e) is spray drying (Deya, page 4, lines 12-13).
Regarding claim 37, modified Silver teaches the invention as described above in claim 7, including the milk powder of step (e) may be used in the product of yogurt (Deya, page 4, lines 44-45). However, the purpose or intended use of the claimed invention which do not result in a structural difference (or, in the case of process claims, manipulative difference) between the claimed invention and the prior art do not limit the claim and do not distinguish over the prior art apparatus (or process). See, e.g., In re Otto, 312 F.2d 937, 938, 136 USPQ 458, 459 (CCPA 1963); In re Sinex, 309 F.2d 488, 492, 135 USPQ 302, 305 (CCPA 1962). If a prior art structure is capable of performing the intended use as recited in the preamble, then it meets the claim. See, e.g., In re Schreiber, 128 F.3d 1473, 1477, 44 USPQ2d 1429, 1431 (Fed. Cir. 1997) and cases cited therein, as it has been held that the recitation of a new intended use for an old product does not make a claim to that old product patentable. In re Schreiber, 44 USPQ2d 1429 (Fed. Cir. 1997). See also MPEP § 2111.02, §2112.02 and 2114-2115. The potential to use the claimed milk powder in the production of a protein bar, a milk drink, an infant formula, or a yogurt does not result in a structural difference between the claimed invention and that of the prior art. The milk powder of the prior art is capable of performing the intended use recited in the claim and thus, meets the limitations of the claim.
Regarding claim 38, modified Silver teaches the invention as described above in claim 7, including the reducing sugar maybe selected from the group consisting of glucose, galactose, and fructose (page 171, 2nd column, 2nd paragraph under section 2.1; page 174, 1st column, 1st paragraph; page 174, 2nd column 2nd paragraph).
Claims 9 and 23-24 are rejected under 35 U.S.C. 103 as being unpatentable over Silver (US 2009/0297660; previously cited) in view of Deya (EP0458358; IDS citation), Larsen (US 2015/0223481; previously cited), and Liu (Liu et al., “Glycation a promising method for food protein modification: Physicochemical properties and structure, a review”, 2012, Food Research International, vol. 49, pages 170-183) as evidenced by search results filed 05/13/2021 as applied to claim 7 above, and further evidenced by ADPI (“Skim Milk Powder (SMP) Standard”, April 2017, American Dairy Products Institute (ADPI), https://web.archive.org/web/20170423045001/https://www.adpi.org/DairyProducts/DryMilks/SkimMilkPowder/tabid/359/Default.aspx; previously cited).
Regarding claim 9, Silver teaches the invention as disclosed above in claim 7, including the milk substrate comprises powdered skim milk [0086], which has a minimum protein content of 34 wt.% protein as evidenced by ADPI (page 1, paragraph 1). Therefore, the milk substrate disclosed by Silver has a total amount of at least 34 wt.% protein, which falls within the claimed protein content range.
Regarding claims 23 and 24, Silver teaches the invention as disclosed above in claim 7, including the milk substrate comprises rehydrated powdered skim milk [0086] and at least 7 wt.% lactose [0024]. Powdered skim milk contains a maximum of 5 wt.% moisture as evidenced by ADPI (page 1, paragraph 1); therefore, it contains 95-100 wt.% solids. As such, the rehydrated skim milk powder of Silver comprises solids from an amount greater than 7 wt.% to an amount less than 100 wt.%, which encompasses the concentrations recited in present claims 23 and 24. The selection of a value within the overlapping ranges renders the claimed concentrations obvious. MPEP 2144.05.I.
Response to Arguments
Claim Rejections – 35 U.S.C. §103 of claims 7, 10-13, 16-22, and 25-37 over Silver, Deya, Larsen, and Sóla: Applicant’s arguments have been fully considered and are considered unpersuasive.
Applicant amended claim 7 to recite that the enzyme having transgalactosylating activity is glycated using specific conditions. Applicant also amended claim 7 to recite a step (f) which is interpreted as described above in the 35 U.S.C. §112(b) rejection. Applicant argued that these new features of amended claim 7 are not disclosed by the combination of Silver, Deya, Larsen, and Sóla. Applicant then argued that the broad statement of “glycosylation by any method seems to induce similar stabilization effects” written on page 7 of the Final Office Action filed 10/20/2025 is not substantiated by the cited references. Applicant argued that a skilled practitioner would not believe that glycosylation does induce similar stabilization effects (Applicant’s Remarks, page 6, 1st-3rd paragraphs under “Claim Rejections Under 35 U.S.C. § 103”).
However, the Examiner points out that Sóla states “Although some of these glycosylation methods (e.g., glycation) may be undesired for use in protein pharmaceuticals their fundamental scientific value for the understanding the effects of glycosylation on protein stability cannot be ignored […] This is due to the fact that independently of the method by which the structurally different glycans are attached to the protein surface (e.g. enzymatic and chemical glycosylation, or reductive glycation) they all seem to induce similar stabilization effects” in the 1st paragraph on page 4. This disclosure provided the basis for the statement “glycosylation by any method seems to induce similar stabilization effects” in the Final Office Action; and as such, provided a basis in a cited reference for a skilled practitioner to believe that different glycosylation methods induce similar stabilization effects. Applicant has not offered any other interpretation for this disclosure and thus, Applicant’s arguments regarding this statement are unpersuasive. The Examiner also notes that Sóla is not cited in the new grounds of rejection for amended claim 7.
Applicant stated that the present specification provides evidence of unexpected results when the enzyme having transgalactosylating activity has been glycated by incubating the enzyme with 55-65% of a reducing sugar for 60-80 hours at a temperature of 50-60°C; and when the milk powder and the glycated enzyme are combined at a temperature of 50-60°C. Applicant pointed to the results shown in Tables 3 and 4 (i.e., results at temperatures of 50-65°C as encompassed by claim 7) as compared to the results of Tables 1 and 2 (i.e., results at a temperature of 5°C which is not encompassed by claim 7). Applicant stated that these results showed GOS production is significantly increased in both regular milk and 60% skim milk powder in the results of Tables 3 and 4 when compared to the results in Tables 1 and 2. Applicant argued that these are unexpected results that are not disclosed by any of the cited references and could not be predicted by one skilled in the art (Applicant’s Remarks, page 6, 3rd paragraphs under “Claim Rejections Under 35 U.S.C. § 103” – page 7, 3rd paragraph).
However, the Examiner points out that claim 7 requires that the milk substrate be reconstituted milk powder or concentrated milk. Since the examples of Tables 1 and 3 use regular milk as the milk substrate, the results of these tables are not encompassed by the present claims. Therefore, Applicant’s arguments regarding Tables 1 and 3 are moot.
In response to Applicant’s assertion that the present specification provides evidence of unexpected results when the enzyme having transgalactosylating activity has been glycated by incubating the enzyme with 55-65% of a reducing sugar for 60-80 hours at a temperature of 50-60°C, Applicant has not stated what results were expected from using an enzyme glycated in this manner. Without a basis of comparison in the form of expected results, it is not clear as to how the claimed glycation method provided unexpected results, especially wherein the specific parameters of the claimed glycation method (i.e., the specific amount of reducing sugar, specific time range, specification temperature range) are not shown to be critical to the claimed invention. “To establish unexpected results over a claimed range, applicants should compare a sufficient number of tests both inside and outside the claimed range to show the criticality of the claimed range. In re Hill, 284 F.2d 955, 128 USPQ 197 (CCPA 1960).” MPEP §716.02(d)II.
In response to Applicant’s assertion that the present specification provides evidence of unexpected results when the milk powder and the glycated enzyme are combined at a temperature of 50-60°C, it is not clear as to what is meant by this limitation as described above in the 35 U.S.C. §112(b) rejection above. Therefore, this feature is being interpreted as meaning that step (b) of the presently claimed method further comprises combining the milk substrate and the glycated enzyme at a temperature of 50-60°C so that the milk powder produced in step (e) of the presently claimed method has an increased amount of GOS compared to a milk powder produced by combining the milk substrate and the glycated enzyme at a temperature of 5°C.
Furthermore, it is noted that that the examples using enzyme treatment temperatures of 50, 55, and 60°C used a treatment time of 24 hours while the example using an enzyme treatment temperatures of 65°C used a treatment time of 3 hours and the example using an enzyme treatment temperatures of 5°C used a treatment time of 22.5 hours (specification, page 32, 4th paragraph – page 33, 1st paragraph). It is also noted that the different temperatures used different amounts of enzyme (specification, Tables 2 and 4). Since different temperatures, times, and enzyme concentrations were used during the step of contacting the milk substrate with the enzyme in the examples of the present specification, it is unclear as to whether the temperature, the time, or the enzyme concentration were responsible for the differing concentrations of DP3+GOS. Therefore, the examples do not support Applicant’s assertion of unexpected results, especially wherein it is known in the art that higher reaction temperatures lead to faster rates of reaction and thus faster creation of reaction products (e.g., a reaction temperature of 50°C produces 10 units of a reaction product in 1 hour wherein a reaction temperature of 5°C for the same reaction produces 1 unit of the same reaction product in 1 hour).
In regard to the cited prior art disclosing the enzyme treatment of the milk substrate in step (b) of the presently claimed method occurring at a temperature of 50-60°C as recited in step (f) of amended claim 7, Silver teaches that the enzyme treatment step may occur at a temperature of about 40°C to about 65°C [0092]. Therefore, the prior art at least suggests that the milk powder produced in step (e) has an increased amount of GOS compared to a milk powder produced by combining the milk substrate and the glycated enzyme at a temperature of 5°C, thereby rendering the claimed increased GOS in the milk powder obvious. Further, the Office does not have laboratory facilities to test claim limitations drawn toward results of practicing the method as claimed. Accordingly, such an increase in GOS produced by the enzyme treatment at 50-60°C in comparison to GOS produced by enzyme treatment at 5°C does not serve to distinguish the method as claimed from the prior art and is thus considered obvious to one having ordinary skill in the art, especially in light of the prior art teaching enzyme treatment at temperatures encompassing 50-60°C.
Since Applicant’s arguments have been shown to be moot or unpersuasive, the rejections of the claims stand as written herein under new grounds of rejection necessitated by the amendment of claim 7.
Conclusion
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/KELLY P KERSHAW/Examiner, Art Unit 1791