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 Request for Continued Examination (RCE under 37 CFR 1.114) and the Response and Amendment filed 1 October 2025 is acknowledged.
Applicant has overcome the following by virtue of amendment of the claims: (1) the objection to claim 14 has been withdrawn; (2) the non-statutory double patenting rejection has been withdrawn.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 1-8, 10-11, and 14-16
Withdrawn claims: None
Previously canceled claims: 9
Newly canceled claims: 12-13
Amended claims: 1 and 14
New claims: None
Claims currently under consideration: 1-8, 10-11, and 14-16
Currently rejected claims: 1-8, 10-11, and 14-16
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 1 October 2025 has been entered.
Claim Rejections - 35 USC § 112
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 6, 8, and 11 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 regards as the invention.
Claim 6 recites the limitation, “wherein the dough further comprises a lipase”. Claim 1 already recites that the dough comprises a lipase. Claim 6 uses the same term “a lipase” to refer to what is ostensibly a further component. It is unclear whether or not claim 6 requires that the dough comprises an additional lipase. The instant specification at paragraphs [8] and [80] appears to convey that the invention comprises only one lipase. However, at paragraphs [72] – [74], and [89], the instant specification appears to provide sufficient support for an embodiment comprising more than one lipase. Applicant can overcome this rejection by cancelling the claim or by amending the claim to recite, “wherein the dough further comprises an additional lipase”, or similar. For purposes of examination, the limitation is construed to recite, “wherein the dough further comprises an additional lipase”.
It is noted that should Applicant choose to cancel claim 6, claim 11 will be subject to rejection under 35 U.S.C. § 112(d) for failing to further limit the subject matter of claim 1 because “at least 80%” is broader, not narrower, than “at least 90%”.
Claims 8 and 11 are rejected due to their dependency from claim 6.
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, 4, 6-7, 10-11, and 14 are rejected under 35 U.S.C. 103 as being unpatentable over Adams et al. (WO 2015/021600 A1, cited on the IDS filed on 1 September 2022) in view of Clausen et al. (WO 98/26057 A1, cited on the IDS filed on 1 September 2022).
Regarding Claim 1, Adams teaches a method for preparing a dough comprising incorporating into the dough a thermotolerant beta-amylase – “…the present teachings relate to the use of a beta amylase in the preparation of…a dough…” (p. 40, lines 19-25). The beta amylase is a purified polypeptide, the amino acid sequence of which comprises a sequence that is at least 81% identical to SEQ ID NO: 3 (claim 6), one of which is the thermostable beta-amylase PspAmy9, (i.e., the protein of SEQ ID NO: 3) (p. 68, lines 14-16). PspAmy9 is demonstrated to have a thermostability of 57 °C (pp. 75-76, Table 4; Figure 4).
wherein said dough comprises flour – (p. 42, lines 14-22),
a monoglyceride emulsifier – “The dough may further comprise an emulsifier such as mono- or diglycerides” and lactic and acetic acid esters thereof (p. 42, line 29 – p. 43, line 4),
a lipase – Adams teaches adding a phospholipase in an amount that improves the softness of the bread (p. 41, line 26 – p. 27, line 13)
and wherein the dough comprises the thermotolerant beta-amylase in an amount of from 1 to 100 ppm by weight based on the weight of the flour – Adams teaches that the beta amylase can be added alone or in combination with other amylases to prevent or retard staling, and the amount of anti-staling amylase will typically be in the range of 0.01-10 mg of enzyme protein per kg of flour (i.e., 0.01-10 ppm) (p. 41, lines 13-16). The claimed range of 1 to 100 ppm overlaps the disclosed range of 0.01 to 10 ppm. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
Adams does not specifically discuss that the amount of monoglyceride emulsifier in the dough is >0 to 0.05 wt%, or teach that the lipase is a polypeptide having lipase activity comprising an amino acid sequence that is at least 90% identical to amino acids 31 to 303 of SEQ ID NO: 11
However, regarding the emulsifier, Adams teaches that a monoglyceride emulsifier may be added to the dough, and also that an emulsifier is not required. “The dough may further comprise an emulsifier such as mono- or diglycerides…In particular the dough can be made without addition of emulsifiers” (p. 42, line 29 – p. 43, line 4). As such, Adams teaches embodiments without an emulsifier and embodiments comprising a monoglyceride emulsifier.
MPEP § 2144.05(I) states, “A range can be disclosed in multiple prior art references instead of in a single prior art reference depending on the specific facts of the case. Iron Grip Barbell Co., Inc. v. USA Sports, Inc., 392 F.3d 1317, 1322, 73 USPQ2d 1225, 1228 (Fed. Cir. 2004). The patent claim at issue was directed to a weight plate having 3 elongated openings that served as handles for transporting the weight plate. Multiple prior art patents each disclosed weight plates having 1, 2 or 4 elongated openings. 392 F.3d at 1319, 73 USPQ2d at 1226. The court stated that the claimed weight plate having 3 elongated openings fell within the ‘range’ of the prior art and was thus presumed obvious. 392 F.3d at 1322, 73 USPQ2d at 1228. The court further stated that the ‘range’ disclosed in multiple prior art patents is ‘a distinction without a difference’ from previous range cases which involved a range disclosed in a single patent since the ‘prior art suggested that a larger number of elongated grips in the weight plates was beneficial… thus plainly suggesting that one skilled in the art look to the range appearing in the prior art.’ Id.”.
By the same logic, where Adams teaches that an emulsifier is an optional ingredient (i.e., the composition contains 0 wt% emulsifier), and where Adams also teaches that the dough may comprise an emulsifier, the range of 0 wt% to any amount is also disclosed. The claimed range of >0 to 0.05 wt% lies inside the disclosed range of 0 wt% to any amount. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I). An appropriate amount of emulsifier could easily be determined by routine experimentation. Absent any evidence of criticality of the claimed range, the limitation is obvious.
Regarding the lipase, Clausen teaches the isolation of a polypeptide variant having lipolytic activity comprising an amino acid sequence that is at least 90% identical the sequence of SEQ ID NO: 11. Clausen teaches a cloned phospholipase having the same sequence as SEQ ID NO: 2 (p. 7, lines 6-20) and variants of preferably not more than one amino acid from the mature part of the amino acid sequence set forth in SEQ ID NO: 2 (p. 38, lines 19-32). The lipase has phospholipase A activity (p. 7, lines 22-30). Clausen further teaches adding the lipase to dough during processes for making bread or other baked products to provide improved properties (p. 47, lines 12-17) such as increased volume, improved crumb structure, and anti-staling properties of the baked product (p. 47, lines 29-39). SEQ ID NO: 2 of Clausen has 100% identity with SEQ ID NO: 11 of the present application. See alignment below:
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Since Adams teaches adding a phospholipase in an amount that improves the softness of the bread (p. 41, line 26 – p. 27, line 13), but is silent as to the specific sequence identity, and Clausen discloses phospholipase enzyme variants suitable for improving dough and/or baked products, it would have been obvious to one of ordinary skill in the art to use the variant of Clausen, comprising an amino acid sequence that is at least 90% identical to amino acids 31 to 303 of SEQ ID NO: 11, as the lipase in the dough composition of Adams, which includes a thermostable beta-amylase, by simple substitution. The substitution would yield the predictable result of a baked product with improved softness, MPEP § 2143(I)(B).
Claim 1 is therefore rendered obvious.
Regarding claim 4, Adams also teaches that the dough comprises 4-80 ppm of the thermotolerant beta amylase – the beta amylase can be added alone or in combination with other amylases to prevent or retard staling, and the amount of anti-staling amylase (i.e., beta-amylase) will typically be in the range of 0.01-10 mg of enzyme protein per kg of flour (i.e., 0.01-10 ppm) (p. 41, lines 13-16). The claimed range of 4-80 ppm overlaps the disclosed range of 0.01-10 ppm. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
Claim 4 is therefore rendered obvious.
Regarding claim 6, Adams also teaches that the dough further comprises an additional lipase – “Optionally, an additional enzyme may be used together with the anti-staling amylase and the phospholipase. The additional enzyme may be…a lipase…” (p. 43, lines 10-22).
Claim 6 is therefore rendered obvious.
Regarding claim 7, Adams also teaches that the dough comprises 0.1-4 ppm lipase – “The amount of phospholipase will typically be in the range of 0.01-10 mg of enzyme protein per kg of flour, e.g., 0.1-5 mg/kg [i.e., ppm]”. (p. 42, lines 7-10). The claimed range of 0.1-4 ppm lies inside the disclosed range of 0.1-5 ppm. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
Claim 7 is therefore rendered obvious.
Regarding claim 10, Adams teaches that the dough may also comprise fat (p. 42, lines 28-29). As fat is an optional ingredient, Adams discloses adding 0 wt-% fat. As 0 wt-% of fat falls within the scope of the claimed range of “up to 4 wt-% fat”, claim 10 is rendered obvious.
Regarding claim 11, Adams and Clausen teach the method according to claim 6.
Adams does not discuss that the lipase is a polypeptide variant having lipolytic activity comprising an amino acid sequence that is at least 80% identical the sequence of SEQ ID NO: 11.
However, as described regarding claim 1 above, Clausen teaches the isolation of polypeptide variants having lipolytic activity comprising an amino acid sequence that is at least 90% identical the sequence of SEQ ID NO: 11, and therefore, also at least 80% identical to the sequence of SEQ ID NO: 11. Clausen teaches a cloned phospholipase having the same sequence as SEQ ID NO: 2 (p. 7, lines 6-20) and variants of preferably not more than one amino acid from the mature part of the amino acid sequence set forth in SEQ ID NO: 2 (p. 38, lines 19-32). The lipase has phospholipase A activity (p. 7, lines 22-30). Clausen further teaches adding the lipase to dough during processes for making bread or other baked products to provide improved properties (p. 47, lines 12-17) such as increased volume, improved crumb structure, and anti-staling properties of the baked product (p. 47, lines 29-39). SEQ ID NO: 2 of Clausen has 100% identity with SEQ ID NO: 11 of the present application (see alignment presented regarding claim 1 above).
Since Adams teaches adding a phospholipase in an amount that improves the softness of the bread (p. 41, line 26 – p. 27, line 13) and that more than one lipase may be added to the dough (p. 43, lines 10-22), but is silent as to the specific sequence identity, and Clausen discloses phospholipase enzyme variants suitable for improving dough and/or baked products, it would have been obvious to one of ordinary skill in the art to add another variant of Clausen, comprising an amino acid sequence that is at least 80% identical to amino acids 31 to 303 of SEQ ID NO: 11, as the additional lipase in the dough composition of Adams by simple substitution. The substitution would yield the predictable result of a baked product with improved softness, MPEP § 2143(I)(B).
Claim 11 is therefore rendered obvious.
Regarding claim 14, Adams also teaches that the thermotolerant beta-amylase is active at a temperature in the range of from 20 to 60 °C – Figure 3 of Adams shows that the thermotolerant beta-amylase PspAmy9 is active at a temperature range of 30 to 95 °C, including 30 to 60 °C, which lies inside the claimed range.
Claim 14 is therefore rendered obvious.
Claims 2-3, 5, and 15-16 are rejected under 35 U.S.C. 103 as being unpatentable over Adams et al. (WO 2015/021600 A1, cited on the IDS filed on 1 September 2022) and Clausen et al. (WO 98/26057 A1, cited on the IDS filed on 1 September 2022) as applied to claims 1 and 6 above, and further in view of Blake et al. (WO 2015/021601 A1).
Regarding claims 2-3, Adams and Clausen teach the method of claim 1.
Adams does not teach that the thermotolerant beta-amylase is a beta-amylase having residual enzymatic activity after exposure to 84 degrees Celsius for 2 hours (re: claim 2) or at least 25% residual activity after exposure to 84 degrees Celsius for 2 hours (re: claim 3). PspAmy9 does not possess this feature (p. 75, Example 7; Figure 4). Adams is silent regarding the thermotolerance of PspAmy9 variants.
However, Blake teaches a thermostable beta-amylase with activity at a temperature range of 80-95 degrees Celsius, and it is used to promote maltose production simultaneously with starch liquefaction (p. 3, lines 27-30). Figure 4 shows that the thermostable beta-amylase is active from 30 to 95 degrees Celsius. As disclosed in Example 3 (p. 25, lines 18-24 – p.26, lines 1-16), the thermostable beta-amylase (TthAmyl) maintains a significant amount of maltogenic activity for 7.5 hours at 80 degrees Celsius (p. 26, lines 13-14). Furthermore, Figure 4 shows that TthAmyl has increased activity at increased temperatures, plateauing at 90 degrees Celsius. Therefore, given that TthAmyl has increased activity at 90 degrees Celsius as compared to 80 degrees Celsius, and that TthAmyl maintains a significant amount of maltogenic activity after 7.5 hours at 80 degrees Celsius, it is presumed that the TthAmyl of Blake would have at least 25% residual enzymatic activity after exposure to 84 degrees Celsius for 2 hours.
It would have been obvious to one of ordinary skill in the art to substitute the thermostable beta-amylase of Blake for the thermostable beta-amylase of Adams because both enzymes are active at the same temperature range (Figure 3 of Adams shows that the thermotolerant beta-amylase PspAmy9 is active at a temperature range of 30 to 95 °C), and are used to achieve the same purpose (i.e., maltose production in a high-temperature environment), MPEP § 2144.06(II). Given that both beta-amylase enzymes are disclosed to have activity at a range of 30-95 degrees Celsius, and the teachings of Example 3 and Figure 4 in Blake, there would be reasonable expectation of success as measured by resultant anti-staling properties of the baked product, MPEP § 2143(I)(B).
Claims 2 and 3 are therefore rendered obvious.
Claim 5 is rejected under 35 U.S.C. 103 as being unpatentable over Adams et al. (WO 2015/021600 A1, cited on the IDS filed on 1 September 2022) and Clausen et al. (WO 98/26057 A1, cited on the IDS filed on 1 September 2022) as applied to claim 1 above, and further in view of Blake et al. (WO 2015/021601 A1).
Regarding claim 5, Adams and Clausen teach the method of claim 1.
Adams does not teach that the beta-amylase is a variant polypeptide having beta-amylase activity, wherein the variant polypeptide is encoded by a nucleic acid sequence that is at least 80% identical to the nucleic acid sequence as set forth in SEQ ID NO: 1. Alignment of the amino acid sequence encoded by the nucleic acid sequence as set forth in SEQ ID NO: 1 with SEQ ID NO: 3 of Adams indicates only 61% identity. See alignment below:
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However, Blake teaches the generation of a thermostable beta-amylase with activity at a temperature range of 80-95 degrees Celsius, and it is used to promote maltose production simultaneously with starch liquefaction (p. 3, lines 27-30). Figure 4 shows that the thermostable beta-amylase is active from 30 to 95 degrees Celsius. The thermostable beta-amylase shares 99.8% identity with SEQ ID NO: 1 (p. 20-21, SEQ ID NO: 3).
See alignment below:
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It would have been obvious to one of ordinary skill in the art to substitute the thermostable beta-amylase of Blake for the thermostable beta-amylase of Adams because both enzymes are active at the same temperature range (Figure 3 of Adams shows that the thermotolerant beta-amylase PspAmy9 is active at a temperature range of 30 to 95 °C), and are used to achieve the same purpose (i.e., maltose production in a high-temperature environment), MPEP § 2144.06(II). Given that both beta-amylase enzymes are disclosed to have activity at a range of 30-95 degrees Celsius, there would be reasonable expectation of success as measured by resultant anti-staling properties of the baked product, MPEP § 2143(I)(B).
Claim 5 is therefore rendered obvious.
Regarding claims 15-16, Adams and Clausen teach the method of claim 6.
Adams does not teach that the thermotolerant beta-amylase is a beta-amylase having residual enzymatic activity after exposure to 84 degrees Celsius for 2 hours (re: claim 15) or at least 25% residual activity after exposure to 84 degrees Celsius for 2 hours (re: claim 16). PspAmy9 does not possess this feature (p. 75, Example 7; Figure 4). Adams is silent regarding the thermotolerance of PspAmy9 variants.
However, Blake teaches a thermostable beta-amylase with activity at a temperature range of 80-95 degrees Celsius, and it is used to promote maltose production simultaneously with starch liquefaction (p. 3, lines 27-30). Figure 4 shows that the thermostable beta-amylase is active from 30 to 95 degrees Celsius. As disclosed in Example 3 (p. 25, lines 18-24 – p.26, lines 1-16), the thermostable beta-amylase (TthAmyl) maintains a significant amount of maltogenic activity for 7.5 hours at 80 degrees Celsius (p. 26, lines 13-14). Furthermore, Figure 4 shows that TthAmyl has increased activity at increased temperatures, plateauing at 90 degrees Celsius. Therefore, given that TthAmyl has increased activity at 90 degrees Celsius as compared to 80 degrees Celsius, and that TthAmyl maintains a significant amount of maltogenic activity after 7.5 hours at 80 degrees Celsius, it is presumed that the TthAmyl of Blake would have at least 25% residual enzymatic activity after exposure to 84 degrees Celsius for 2 hours.
It would have been obvious to one of ordinary skill in the art to substitute the thermostable beta-amylase of Blake for the thermostable beta-amylase of Adams because both enzymes are active at the same temperature range (Figure 3 of Adams shows that the thermotolerant beta-amylase PspAmy9 is active at a temperature range of 30 to 95 °C), and are used to achieve the same purpose (i.e., maltose production in a high-temperature environment), MPEP § 2144.06(II). Given that both beta-amylase enzymes are disclosed to have activity at a range of 30-95 degrees Celsius, and the teachings of Example 3 and Figure 4 in Blake, there would be reasonable expectation of success as measured by resultant anti-staling properties of the baked product, MPEP § 2143(I)(B).
Claims 15 and 16 are therefore rendered obvious.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Adams et al. (WO 2015/021600 A1, cited on the IDS filed on 1 September 2022) and Clausen et al. (WO 98/26057 A1, cited on the IDS filed on 1 September 2022) as applied to claims 1 and 6 above, and further in view of Tsutsumi et al. (WO 02/00852 A2).
Regarding claim 8, Adams and Clausen teach the method according to claim 6.
The cited prior art does not discuss that the lipase is a variant polypeptide of the lipase of SEQ ID NO: 10 having lipase activity and comprising an amino acid sequence which is at least 80% identical to the sequence of SEQ ID NO: 10.
However, Tsutsumi teaches the isolation of a polypeptide variant having lipolytic activity comprising an amino acid sequence that is at least 80% identical the sequence of SEQ ID NO: 10. Tsutsumi discloses that this polypeptide is a variant of the Fusarium solani sequence, and that it has phospholipase and galactolipase lipolytic activity (p. 32, lines 11-22; pp. 62-63, SEQ ID NO: 10, 97.3%).
See alignment below:
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Since Adams teaches adding a phospholipase in an amount that improves the softness of the bread (p. 41, line 26 – p. 27, line 13) and that more than one lipase may be added to the dough (p. 43, lines 10-22), but is silent as to the specific sequence identity, and Tsutsumi discloses additional lipolytic enzyme variants, it would have been obvious to one of ordinary skill in the art to add the variant of Tsutsumi, comprising an amino acid sequence that is at least 80% identical to the sequence of SEQ ID NO: 10, as the additional lipase in the dough composition of Adams by simple substitution. The substitution would yield the predictable result of a baked product with improved softness, MPEP § 2143(I)(B).
Claim 8 is therefore rendered obvious.
Response to Arguments
Claim Objections:
Applicant has overcome the objection to claim 14 by amendment. Accordingly, the objection has been withdrawn.
Claim Rejections – 35 U.S.C. § 102: Applicant’s amendment to claim 1, filed on 1 October January 2025, is sufficient to overcome the 35 U.S.C. § 102 rejection. Accordingly, the rejection has been withdrawn. However, upon further consideration, claim 1 is rejected under 35 U.S.C. § 103 as described hereinabove.
Claim Rejections – 35 U.S.C. § 103: Applicant’s arguments filed on 1 October 2025 have been fully considered, but they are not persuasive.
Applicant first argued that the inventors of the claimed invention have surprisingly found that the incorporation of the claimed thermotolerant beta-amylase into a dough product shows significant improvements in hardness and resilience over time when tested compared to previously commercially available beta-amylase, citing Figure 1B. Applicant continues that it is even more surprising that the use of such a beta-amylase shows significantly improved results even in the absence of a monoglyceride emulsifier, citing Figure 2. Applicant asserted that this effect would not have been expected (p. 7, ¶ 2).
Applicant’s surprising discovery that the incorporation of a thermotolerant beta-amylase into a dough product improves hardness and resilience both in the presence and absence of a monoglyceride emulsifier is acknowledged, but it is not found to be persuasive. MPEP § 2145 states, “If a prima facie case of obviousness is established, the burden shifts to the applicant to come forward with arguments and/or evidence to rebut the prima facie case. See, e.g., In re Dillon, 919 F.2d 688, 692, 16 USPQ2d 1897, 1901 (Fed. Cir. 1990) (en banc)”, and “[r]ebuttal evidence may include evidence of ‘secondary considerations,’ such as ‘commercial success, long felt but unsolved needs, [and] failure of others.’ Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 4459, 467. See also, e.g., In re Piasecki, 745 F.2d 1468, 1473, 223 USPQ 785, 788 (Fed. Cir. 1984) (commercial success). Rebuttal evidence may also include evidence that the claimed invention yields unexpectedly improved properties or properties not present in the prior art. Rebuttal evidence may consist of a showing that the claimed compound possesses unexpected properties. Dillon, 919 F.2d at 692-93, 16 USPQ2d at 1901. A showing of unexpected results must be based on evidence, not argument or speculation. In re Mayne, 104 F.3d 1339, 1343-44, 41 USPQ2d 1451, 1455-56 (Fed. Cir. 1997)”. However, as provided by MPEP § 2145(II), “[m]ere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention. In re Wiseman, 596 F.2d 1019, 201 USPQ 658 (CCPA 1979)”, and “‘[t]he fact that appellant has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious.’ Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985)”. Furthermore, “[e]vidence of unexpected results must be weighed against evidence supporting prima facie obviousness in making a final determination of the obviousness of the claimed invention. In re May, 574 F.2d 1082, 197 USPQ 601 (CCPA 1978).” See MPEP § 716.02(c)(I). “‘Expected beneficial results are evidence of obviousness of a claimed invention, just as unexpected results are evidence of unobviousness thereof.; In re Gershon, 372 F.2d 535, 538, 152 USPQ 602, 604 (CCPA 1967)”. See MPEP § 716.02(c)(II).
“Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the ‘objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support.’ In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range. In re Clemens, 622 F.2d 1029, 1036, 206 USPQ 289, 296 (CCPA 1980)”. See MPEP § 716.02(d).
In the instant case, a showing of “surprising” results is not substantiated by sufficient evidence. As described in the rejection, Adams and Clausen teach the method of claim 1. Blake teaches a thermostable beta-amylase with 99.8% identity to the peptide sequence corresponding to translated SEQ ID NO:1, with activity over a range of temperatures from 30 to 95 °C (Figure 4), an obvious substitution for the thermotolerant beta-amylase in the method disclosed by Adams, as described regarding claim 5. Therefore, the claimed method was known before the effective filing date of the claimed invention.
Applicant points to Figure 1B as evidence of a surprising effect of adding the claimed beta-amylase to a dough. However, it is noted that BA2 corresponds to SEQ ID NO: 9 (specification [11]), which is a variant of SEQ ID NO: 2 (specification [44]), and this variant is not specifically claimed. As such, Applicant’s evidence is not commensurate in scope with the claimed invention. Further, the comparison between BA2 and 3D in Figure 1B is not a like-for-like comparison as BA2 is a beta-amylase, and, according to the manufacturer’s website, Novamyl 3D is a maltogenic alpha-amylase. The extent of Applicant’s arguments are only of concern to the data of Figure 2A, which is the same as the data presented in Figure 1B. Absent a direct comparison to known thermotolerant beta amylases, and specifically the thermotolerant beta amylase of Blake as described hereinabove, the evidence presented by the specification is not persuasive.
Applicant next argued, separately regarding claims 2 and 3, that the Examiner asserted in part that the residual activity requirement specified there would have necessarily been present in the amylases disclosed in the prior art (p. 7, ¶ 3).
However, this is not the case. The Examiner did not assert that the residual activity would have necessarily been present. The Office Action states that given the teachings of Blake, “it is presumed that the TthAmyl of Blake would have residual activity” as claimed. Without direct evidence to the contrary, provided the teachings of Blake in Figure 4, it is reasonable to expect that the thermotolerant amylase would have residual activity. Figure 4 of Blake indicates that the beta-amylase gains activity as a function of temperature, plateauing at about 90 °C. Blake further teaches in Example 3 (p. 25, lines 18-24 – p.26, lines 1-16), that the thermostable beta-amylase (TthAmyl) maintains a significant amount of maltogenic activity for 7.5 hours at 80 °C (p. 26, lines 13-14). The fact that the TthAmyl maintains significant activity for 7.5 hours at 80 °C and also increases in activity with increasing temperature indicates stability of the enzyme. Therefore, it is seen as a reasonable presumption that the TthAmyl would have residual activity after exposure to 84 °C for 2 hours, and also that the amount of residual activity would be at least 25%. In view of these facts, it is seen that the Office has demonstrated a prima facie case of obviousness, and the burden of proof shifts to the Applicant to prove that the TthAmyl does not exhibit the claimed properties. Furthermore, Applicant demonstrates no evidence of criticality that the residual activity of the beta-amylase must be above 25%.
For at least these reasons, Applicant’s arguments are not found to be persuasive. Claims 1-8, 10-11, and 14-16 are rejected.
Claim Rejections – Double Patenting: Applicant’s amendment to claim 1 to include the limitations of claim 12 is sufficient to overcome the double patenting rejection. Accordingly, the nonstatutory double patenting rejection has been withdrawn.
Conclusion
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/JAMES P. SHELLHAMMER/Examiner, Art Unit 1793
/EMILY M LE/Supervisory Patent Examiner, Art Unit 1793