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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 18 August 2026 has been entered.
Claim Objections
The numbering of claims is not in accordance with 37 CFR 1.126 which requires the original numbering of the claims to be preserved throughout the prosecution. When claims are canceled, the remaining claims must not be renumbered. When new claims are presented, they must be numbered consecutively beginning with the number next following the highest numbered claims previously presented (whether entered or not).
In this case, the newly added claims filed 18 September 2026 are both number “23”. Misnumbered claim 23 been renumbered 24.
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 1-3, 5-13 and 19-24 are rejected under 35 U.S.C. 103 as being unpatentable over Feng et al (herein referred to as Feng, US 20160007618 A1) in view of Shows et al. (herein referred to as Shows, CA 03098718 A1) .
With regard to Claim 1, Feng teaches a method for producing a baked product (abstract). The method comprises providing a dough comprising a mature thermostable amylase ([0016]) and baking the dough to produce a baked product ([0015]).
However, Feng is silent to the amylase being a mature thermostable variant of a parent glucoamylase at least 80% identical to SEQ ID NO:1, SEQ ID NO:6, SEQ ID NO:7 or SEQ ID NO:8.
Shows teaches processes for enhancing yeast growth and/or productivity (page 1 lines 7-8). Shows teaches the yeast can contain an amylase, and more specifically a glucoamylase (page 31 lines 20-25 lines 34-35). Shows teaches mature thermostable variants of a parent glucoamylase with at least a 80% sequence identity to the mature polypeptide (page 76 line 31 – page 77 line 8). The mature polypeptide SEQ ID NOs: 21 in Shows is equivalent to SEQ ID NO: 1 in the instant application. Shows teaches the variants have reduced sensitivity to protease degradation and have improved thermostability compared to the parent (page 77 lines 20-24). Shows teaches the yeast has applications including baking (page 25 line 30).
It would have been obvious to one with ordinary skill in the art before the effective filing date of the claimed invention to modify Feng to utilize the mature thermostable variants of a parent glucoamylase with at least a 80% sequence identity to the mature polypeptide as taught it Shows because the variants have reduced sensitivity to protease degradation and have improved thermostability compared to the parent.
Continuing, Feng is silent to the mature variant comprising at least one amino acid modification, wherein the modification is a substitution, in one or more or all of the positions corresponding to positions 1, 2, 4, 6, 7, 11, 31, 34, 65, 79, 132, 327, 445, 447, 481, 566, 568, 594 and 595 in SEQ ID NO:1.
Shows teaches the glucoamylase has an amino acid modification at position 79 (Page 76 lines 24-25). Shows teaches the modification is a substitution at position 79. (page 76 lines 24-25). Shows teaches the mutant glucoamylase has reduced sensitivity to protease degradation and has improved thermostability compared to the parent (page 77 lines 15-16)
It would have been obvious to one with ordinary skill in the art before the effective filing date of the claimed invention to modify Feng to utilize the glucoamylase with an amino acid modification, specifically a substitution, at position 79 because the variants have reduced sensitivity to protease degradation and have improved thermostability compared to the parent.
Next, Feng is silent to s a substitution at a position corresponding the position 103 of SEQ ID NO: 1, wherein the substitution is to an asparagine.
Shows teaches the glucoamylase has an amino acid modification at position 79 (Page 76 lines 24-25) and further comprises the following combination of substitutions P2N + P4S + P11F + T65A + S103N (emphasis added) + Q327F + E501 V + Y504T (page 78 lines 14-15). Shows teaches the variants have reduced sensitivity to protease degradation and have improved thermostability compared to the parent (page 77 lines 20-23)
It would have been obvious to one with ordinary skill in the art before the effective filing date of the claimed invention to modify Feng to utilize the glucoamylase with an amino acid modification at position 103 with an asparagine as taught by Shows because the variants have reduced sensitivity to protease degradation and have improved thermostability compared to the parent.
With regard to the thermostability improvement (Td), Shows teaches the glucoamylase has an amino acid modification at position 79 (Page 76 lines 24-25) and more specifically Shows teaches the modification is a K79V substitution as stated in instant claims 19-21 (page 76 lines 24-25). Also Shows teaches a substitution at position 103 where the substitution is to an asparagine (page 78 lines 14-15). Shows teaches these variant have improved thermostability compared to the parent (page 76, lines 22-23).
Therefore, Shows teaches the claimed method and thus the resulting product would inherently have the claimed increase in thermostability, See MPEP 2112.01(I) which teaches where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). Not only are the compositions substantially identical, Shows explicitly states there is an increase in thermostability and therefore imparts reasoning for obviousness. See MPEP 2144.07 that discussed that when the prior art recognizes something is suitable for a similar intended use/purpose, such a thing is obvious.
With regard to Claim 2, Feng teaches wherein the baked or par-baked product is a type of bread ([0043]).
With regard to Claim 3, Feng is silent to wherein the parent glucoamylase is from a species of Penicillium.
Shows teaches thermostable glucoamylase is preferably of fungal origin, preferably a filamentous fungi, such as from a strain of the genus Penicillium (page 76, lines 31-34).
Thus, Shows imparts reasoning for obviousness because the teaching shows that glucoamylase from a strain of the genus Penicillium was known for to be successfully utilized and published at the time of filing, which means it was within the general skill of one with ordinary skill in the art to selected a glucoamylase from a strain of the genus Penicillium, because it would be obvious to one of skill in the art to do such a thing on the basis of its suitability for a similar intended use. See MPEP 2144.07 that discussed that when the prior art recognizes something is suitable for a similar intended use/purpose, such a thing is obvious.
With regard to Claims 5-7, Feng is silent to the mature variant comprising at least one amino acid modification, wherein the modification is a substitution, in one or more or all of the positions corresponding to positions 1, 2, 4, 6, 7, 11, 31, 34, 65, 79, 132, 327, 445, 447, 481, 566, 568, 594 and 595 in SEQ ID NO:1.
Shows teaches the glucoamylase has an amino acid modification at position 79 (Page 76 lines 24-25). Shows teaches the modification is a substitution at position 79. (page 76 lines 24-25). Shows teaches the mutant glucoamylase has reduced sensitivity to protease degradation and has improved thermostability compared to the parent.
It would have been obvious to one with ordinary skill in the art before the effective filing date of the claimed invention to modify Feng to utilize the glucoamylase with an amino acid modification, specifically a substitution, at position 79 because the variants have reduced sensitivity to protease degradation and have improved thermostability compared to the parent.
With regard to Claim 8, Feng is silent to the mature thermostable variant has a thermostability improvement (Td) over its parent of at least 50C.
Shows teaches the glucoamylase has an amino acid modification at position 79 (Page 76 lines 24-25) and more specifically Shows teaches the modification is a K79V substitution as stated in instant claims 19-21 (page 76 lines 24-25). Further shows teaches a substitution at position 103 of an asparagine (page 78 lines 14-15). Shows teaches these variant have improved thermostability compared to the parent (page 76, lines 22-23).
Therefore, Shows teaches the claimed method and thus, the resulting product would inherently have the claimed increase in thermostability, See MPEP 2112.01(I) which teaches where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). Not only are the compositions substantially identical, Shows explicitly states there is an increase in thermostability and therefore imparts reasoning for obviousness. See MPEP 2144.07 that discussed that when the prior art recognizes something is suitable for a similar intended use/purpose, such a thing is obvious.
With regard to Claim 9, Feng is silent to wherein the mature thermostable variant has a relative activity at 910C of at least 150 compared to its parent.
Shows teaches the glucoamylase has an amino acid modification at position 79 (Page 76 lines 24-25) and more specifically Shows teaches the modification is a K79V substitution as stated in instant claims 19-21 (page 76 lines 24-25). Further shows teaches a substitution at position 103 of an asparagine (page 78 lines 14-15). Shows teaches these variant have improved thermostability compared to the parent (page 76, lines 22-23).
Therefore, Shows teaches the claimed method, including the specific modifications listed in instant claims 19-21, and thus, the resulting product would inherently have the claimed increase in thermostability, See MPEP 2112.01(I) which teaches where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977)
With regard to Claim 10 and 11 The combination of Yeng and Shows teaches the claimed method and therefore, the resulting product would inherently have the claimed results, See MPEP 2112.01(I) which teaches where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).
With regard to Claim 12, Yeng is silent to wherein the mature thermostable variant glucoamylase enzyme is comprised in the dough in an amount of 0.01- 1,000 mg enzyme protein (mgEP) per kg flour.
Shows teaches the carbohydrate-source generating enzyme, in particular glycoamylase, may be added in amounts from 0.1- 100 micrograms EP/g DS, such as 0.5-50 micrograms EP/g DS, 25 such as 1-25 micrograms EP/g DS, such as 2-12 micrograms EP/g DS (page 79 lines 23-25). One with ordinary skill in the art would recognize the unit micrograms EP/g DS is micrograms per g of dry solids. In this case the dry solids would be flour. Converting the units to what is presented in the instant application, the range taught by Feng is converted to 100 – 100,000 micrograms EP/kg DS. See MPEP 2144.05(I) In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976). Shows teaches the term "carbohydrate-source generating enzyme" includes any enzymes generating fermentable sugars. A carbohydrate-source generating enzyme is capable of producing a carbohydrate that can be used as an energy-source by the fermenting organism(s) (page 76 lines 18-21)
It would have been obvious to one with ordinary skill in the art to modify Feng in view of Shows to include the glucoamylase in an amount in amounts from 0.1- 100 micrograms EP/g DS to generate fermentable sugars.
With regard to Claim 13, Feng teaches the dough also comprises one or more additional enzymes (Claim 1, Feng reads such that the dough comprises a thermally-stable amyloglucosidase and an enzyme selected from the group consisting of: raw starch degrading amyloglucosidases; anti-staling amylases; and mixtures thereof). Feng teaches the additional enzyme can be a maltogenic amylase ([0068]).
With regard to Claims 19-21, Feng is silent to wherein the at least one amino acid modification comprises a substitution in one or more or all of the positions corresponding to R1A, P2N, P4S, P11F, T65A, K79V and Q327F in SEQ ID NO:1.
Shows teaches the glucoamylase has an amino acid modification at position 79 (Page 76 lines 24-25). Shows teaches the modification is a K79V substitution (page 76 lines 24-25) Shows teaches the mutant glucoamylase has reduced sensitivity to protease degradation and has improved thermostability compared to the parent.
It would have been obvious to one with ordinary skill in the art before the effective filing date of the claimed invention to modify Yeng to include the K79V substitution taught by Shows to reduce the sensitivity to protease degradation and improve the thermostability compared to the parent.
With regard to Claim 22, Feng teaches wherein the baked or par-baked product is a type of bread such as pretzels, English muffins, buns, rolls, tortillas (both corn and flour), pizza dough, bagels, and crumpets. ([0043]).
With regard to Claims 23 and 24, Feng is silent to wherein the mature thermostable variant is at least 90% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO:6, SEQ ID NO:7 or SEQ ID NO:8.
Shows teaches mature thermostable variants of a parent glucoamylase with at least a 90% sequence identity to the mature polypeptide (page 76 line 31 – page 77 line 8). The mature polypeptide SEQ ID NOs: 21 in Shows is equivalent to SEQ ID NO: 1 in the instant application.
It would have been obvious to one with ordinary skill in the art before the effective filing date of the claimed invention to modify Feng to utilize the mature thermostable variants of a parent glucoamylase with at least a 90% sequence identity to the mature polypeptide as taught it Shows because the variants have reduced sensitivity to protease degradation and have improved thermostability compared to the parent.
Response to Arguments
Applicant's arguments filed 18 September 2026 have been fully considered but they are not persuasive.
Applicant argues neither feng nor show teach or suggest, alone or in combination, a glucoamylase variant which has a thermostability improvement (Td) over its parent of at least 40C and which further comprises an asparagine substitution at position 103 and is at least 80% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO:6, SEQ ID NO:7 or SEQ ID NO:8. This is not found to be persuasive because Shows teaches a glucoamylase with an amino acid modification at position 79 (Page 76 lines 24-25) and further comprises the following combination of substitutions P2N + P4S + P11F + T65A + S103N (emphasis added) + Q327F + E501 V + Y504T (page 78 lines 14-15). The substitution at position 103 taught by Show is identical to the substitution taught by applicant on page 9 line 12 of the specification. It is important to note that the combination of substitutions at positions 2, 4, 11, 65 and 327 are also claimed by applicant in claim 1. The claim also does not further limit the presence or amount of additional amino acid modifications. With regard to the sequence identity, Shows teaches In an embodiment the thermostable glucoamylase has at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 91 %, more preferably at least 92%, even more preferably at least 93%, most preferably at least 94%, and even most preferably at least 95%, such as even at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to the mature polypeptide shown in SEQ ID NO: 2 in WO 2011/127802 or SEQ ID NOs: 21 herein (page 76 lines 3-8). Lastly, with regard to the thermostability improvement, the combination of Feng and Shows teaches all the claimed limitations and substantially the same composition. Further Shows teaches Shows teaches these variant have improved thermostability compared to the parent (page 76, lines 22-23). Therefore, the composition taught by the combination of Feng and Shows would inherently have the claimed thermostability improvement over its parent. See MPEP 2112.01(I) which teaches where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).
Therefore, applicant’s arguments are not found to be persuasive.
Conclusion
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/K.I.D./Examiner, Art Unit 1792
/ERIK KASHNIKOW/Supervisory Patent Examiner, Art Unit 1792
