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 .
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 19-22 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 70% 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 70% sequence identity to the mature polypeptide (page 76 line 31 – page 77 line 8). The “mature polypeptide Shows in 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 70% 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, 103, 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 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). 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). 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)
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, 103, 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, Yeng is silent to the mature thermostable variant has a thermostability improvement (Td) over its parent of at least 30C.
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). 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). 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, Yeng 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).
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, Yeng 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]).
Response to Arguments
Applicant's arguments filed 24 April 2026 have been fully considered but they are not persuasive.
Applicant argues that the variant taught by Feng and Shows would be unpredictable and unobvious. This argument is not found to be persuasive because Feng is relied upon to teach the claimed dough composition with a mature thermostable glucoamylase (Feng, [0016]). While Shows is then further relied upon to teach the thermostable glucoamylase variant. Shows clearly teaches mature thermostable variants of a parent glucoamylase with at least a 70% sequence identity to the mature polypeptide (page 76 line 31 – page 77 line 8). The “mature polypeptide Shows in SEQ ID NOs: 21 in Shows is equivalent to SEQ ID NO: 1 in the instant application. Then further Shows teaches the identical amino acid modification at position 79 as limited in claim 1 (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). In addition shows provides ample motivation to use these variants with the described amino acids modifications. Shows teaches these variant have improved thermostability compared to the parent (page 76, lines 22-23). As a result Shows teaches a mature thermostable glucoamylase variant that is identical to what is instantly claimed. Per MPEP 2112.01(II) "Products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Therefore, the variant taught by Shows would function the same as the instantly claimed variant and thus not be “unpredictable” or “non-obvious”. Applicants are argument is not found to be persuasive.
Conclusion
THIS ACTION IS MADE FINAL. 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.
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/K.I.D./Examiner, Art Unit 1792
/ERIK KASHNIKOW/Supervisory Patent Examiner, Art Unit 1792
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