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 Application
Receipt of the Response and Amendment after Non-Final Office Action filed 12/19/2025 is acknowledged.
Applicant has overcome the following rejections by virtue of the amendment or cancellation of the claims: (1) the 35 U.S.C. 112(b) rejections of claims 1-9 have been withdrawn; (2) the 35 U.S.C. 103 rejections of claims 1, 3, 4, and 7-11 over Te Poele et al. have been withdrawn; (3) the 35 U.S.C. 103 rejection of claim 2 over Te Poele et al., Nambiar et al., and admitted prior art has been withdrawn; and (4) the 35 U.S.C. 103 rejections of claims 5 and 6 over Te Poele et al. and Poulsen et al. have been withdrawn;
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 1-11
Withdrawn claims: None
Previously canceled claims: None
Newly cancelled claims: 8-11
Amended claims: 1, 2, 3, 5, and 7
New claims: 12-19
Claims currently under consideration: 1-7 and 12-19
Currently rejected claims: 1-7 and 12-19
Allowed claims: None
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 1-7 and 12-19 are rejected under 35 U.S.C. 103 as being unpatentable over Markosyan et al. (U.S. 2014/0357588 A1) in view of Li et al. (U.S. 2019/0078063 A1) and admitted prior art.
Regarding claims 1 and 2, Markosyan et al. discloses a method of glucosylating a steviol glycoside (Fig. 3; p. 99, claim 2), the method comprising providing a composition that comprises at least water ([0159]), sucrose ([0119], [0127], [0171]), a steviol glycoside that comprises stevioside or rebaudioside A ([0048], Fig. 3, [0346]), and a glucosyltransferase enzyme ([0157]), wherein at least one glucosylated form of the steviol glycoside is produced in the composition ([0165], [0166]).
Markosyan et al. does not specifically disclose the glucosyltransferase enzyme as synthesizing alpha-1,3-glucan, wherein at least about 95% of the glycosidic linkages of the alpha-1,3-glucan are alpha-1,3 linkages (claim 1) or the enzyme as comprising the sequences of those specifically claimed (claim 2).
However, the present specification admits that enzyme SEQ ID NO:4 of Li et al. produces ~100% of glycosidic linkages in the alpha-1,3-glucan as alpha-1,3 linkages (p. 24, l. 31 – p. 25, l. 10) and that SEQ ID NO:4 OF Li et al. corresponds to SEQ ID NO:5 of the present specification (p. 27, l. 11 – l. 20), which would constitute an enzyme that comprises an amino acid sequence that is at least 90% identical to residues 55-960 of SEQ ID NO:5.
It would have been obvious to one having ordinary skill in the art to utilize the enzyme taught in Li et al. in the method of Markosyan et al. First, Markosyan et al. says: “The UDP-glucosyltransferase can be any UDP-glucosyltransferase capable of adding at least one glucose unit to the steviol and or steviol glycoside substrate to provide the target steviol glycoside.” ([0157]). Such broad instruction regarding suitable enzymes would suggest to a skilled practitioner that only the function of the enzyme—capability for adding a glucose unit to a steviol/steviol glycoside substrate—is the determining factor as to whether an enzyme would be suited for use in the method of Markosyan et al. As such, any enzyme that exhibited such capability would be obvious to a skilled practitioner. Li et al. is specifically directed to glucosyltransferases ([0002], [0022], [0015]). Thus, utilization of a glucosyltransferase as taught in Li et al. in the method of Markosyan et al. would be obvious. The present specification admits that such enzymes, including SEQ ID NO:4 ([0011], Table 1), produce ~100% of glycosidic linkages in the alpha-1,3-glucan as alpha-1,3 linkages (p. 24, l. 31 – p. 25, l. 10) and that SEQ ID NO:4 OF Li et al. corresponds to SEQ ID NO:5 of the present specification (p. 27, l. 11 – l. 20), which would constitute an enzyme that comprises an amino acid sequence that is at least 90% identical to residues 55-960 of SEQ ID NO:5. The claimed methods comprising a glucosyltransferase that synthesizes alpha-1,3-glucan with at least 95% alpha-1,3-glucan glycosidic linkages (claim 1) and that comprises an amino acid sequence that is at least 90% identical to residues 55-960 of SEQ ID NO:5 would therefore be obvious to a skilled practitioner.
As for claim 3, the incorporation of the glucosyltransferase as taught in Li et al. into the method of Markosyan et al. as described in relation to claims 1 and 2 would result in the alpha-glucan as being produced in the composition.
As for claim 4, Markosyan et al. discloses the composition as being a food product/precursor ([0256]).
As for claim 5, Markosyan et al. discloses the food product/precursor as being a dairy food product (i.e., a yogurt drink) ([0257]).
As for claim 6, Markosyan et al. discloses the food product as being alcoholic beverages, yogurt drinks, or fermented soybean paste ([0257]), which renders a step of fermenting the food product/precursor after providing the initial ingredients obvious.
As for claim 7, Markosyan et al. discloses the steviol glycoside as being present as part of a stevia sweetener ([0118], [0346], [0002]-[0004]).
As for claim 12, the present specification admits that the enzyme disclosed in Li et al. produces about 100% of the glycosidic linkages of the alpha-1,3-glucan as alpha-1,3 linkages (p. 24, l. 31 – p. 25, l. 10).
As for claim 13, incorporation of the enzyme of Li et al. into the method of Markosyan et al. would result in the enzyme being the only glucosyltransferase enzyme in the composition.
As for claim 14, the present specification admits that enzyme SEQ ID NO:4 OF Li et al. corresponds to SEQ ID NO:5 of the present specification (p. 27, l. 11 – l. 20), which would constitute an enzyme that comprises an amino acid sequence that is at least 90% identical to SEQ ID NO:5.
As for claim 15, the present specification admits that enzyme SEQ ID NO:4 OF Li et al. corresponds to SEQ ID NO:5 of the present specification (p. 27, l. 11 – l. 20), as well as that SEQ ID NO:3 and SEQ ID NO:4 are modifications of SEQ ID NO:5, having 9-15 substitutions (p. 28, l. 4 – l. 23). Li et al. discloses that any amino acid sequence that is at least 40% identical to SEQ ID NO:4 that still synthesizes alpha-glucan comprising 1,3-linkages falls within the scope of its disclosure ([0010]). Since the claimed glucosyltransferase enzymes would fall within the scope of the disclosure of Li et al., using one or more glucosyltransferase enzyme that comprises SEQ ID NO:3 or SEQ ID NO:4 would be obvious to a skilled practitioner.
As for claim 16, Markosyan et al. discloses the food product as being a yogurt product ([0257]).
As for claim 17, Markosyan et al. discloses the food product as being a yogurt drinks ([0257]), which renders a step of fermenting the food product/precursor after providing the initial ingredients obvious.
As for claim 18, Markosyan et al. discloses the food product as being a yogurt product ([0257]).
As for claim 19, Markosyan et al. discloses the composition as further comprising rebaudioside D ([0257]).
Response to Arguments
Specification: The objection to the specification has been withdrawn in light of the newly-submitted abstract.
Claim Rejections - 35 U.S.C. § 112: Applicant has overcome the 35 U.S.C. § 112(b) rejections of claims 1-9 based on amendments to the claims. Accordingly, the 35 U.S.C. § 112(b) rejections have been withdrawn.
Claim Rejections - 35 U.S.C. § 103 of claims 1, 3, 4, and 7-11 over Te Poele et al.; claim 2 over Te Poele et al., Nambiar et al., and admitted prior art; and claims 5 and 6 over Te Poele et al. and Poulsen et al.: Applicant’s arguments (Applicant’s Remarks, p. 7, ¶3 – p. 9, ¶5) have been considered but are moot because the new grounds of rejection do not rely on any reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument.
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.
Claims 1-7 and 12-19 are rejected.
No claims are allowed at this time.
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/JEFFREY P MORNHINWEG/Primary Examiner, Art Unit 1793
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