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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 08/24/2026 has been entered.
Response to Arguments
Applicant’s arguments with respect to claims 1, 3-6, 8-12, and 14-21 have been considered but are moot in view of a new grounds of rejection necessitated by the amendments to the claims.
Claim Objections
Claim 20 is objected to because of the following informalities:
In claim 20, it is believed “the polypeptide having lipoxygenase activity” should read “the lipoxygenase” to match the style of claim 10, from which it depends.
Appropriate correction is required.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1, 3-4, 6, 9, 11, 14-16, and 19 are rejected under 35 U.S.C. 103 as being unpatentable over Hage et al. (US Patent Application Publication 2003/0166485) (already of record) in view of Salmon et al. (US Patent Application Publication 2006/0042020) (already of record).
Regarding claim 1, Hage et al. discloses a method for bleaching a stain on a textile (para. 10-15, 21), the method comprising contacting the textile with a wash liquor (para. 21, 94-95), wherein the wash liquor comprises a polypeptide having lipoxygenase activity (para. 57, 95) and further comprises detergent in the wash liquor (para. 90-94), and a lipase (para. 66, 95).
Hage et al. is silent as to the particular range of about 0.1-2.0 g detergent/L wash liquor, and is silent as to the wash liquor comprising one or more polyunsaturated fatty acids.
As to the limitation regarding the range amount of detergent in the wash liquor, it has been held that where 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, when the particular parameter is recognized as a result-effective variable (MPEP §2144.05). Hage et al. discloses general conditions for the grams of detergent per liter of wash liquor (para. 90-95), and the skilled artisan would clearly recognize the amount of detergent per liter of wash liquor as a result-effective variable, as this parameter would affect the cleaning activity as is notoriously well known in the art. Therefore, it would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to discover an optimum or workable range by routine experimentation.
As to the limitation regarding the one or more polyunsaturated fatty acids, Hage et al. discloses that it was known in the art to use an unsaturated fatty acid and lipoxygenase in solution in a process for bleaching a stain (para. 3).
Furthermore, Salmon et al. discloses that lipoxygenase activity during textile bleaching is enhanced by the addition of linoleic acid (reads on a polyunsaturated fatty acid) (para. 85-88, 208-210, 216-220).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the method disclosed by Hage et al. such that the wash liquor comprises linoleic acid (reads on one or more polyunsaturated fatty acids), based on the teachings of Salmon et al., in order to enhance the lipoxygenase activity during textile bleaching.
Regarding claim 3, Hage et al. discloses wherein the polypeptide having lipoxygenase activity is a soybean lipoxygenase (para. 95).
Regarding claim 4, Hage et al. discloses wherein the polypeptide having lipoxygenase activity is a soybean lipoxygenase (para. 95).
Hage et al. does not expressly teach wherein the soybean lipoxygenase is soybean lipoxygenase 1 (LOX-1).
Salmon et al. discloses use of lipoxygenase in a method of textile bleaching, as discussed above. Salmon et al. discloses wherein the lipoxygenase may be derived from various sources such as a soybean (para. 82), and further discloses wherein the lipoxygenase is classified as EC 1.13.11.12 (para. 79), which is synonymous with soybean lipoxygenase 1 (LOX-1) (see p. 5 of the prior Non-Final Rejection dated 11/24/2025 and the UniProt entry for EC 1.13.11.12 which has been made of record).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the method disclosed by Hage et al. such that the soybean lipoxygenase is soybean lipoxygenase 1, based on the disclosure of Salmon et al., as the skilled artisan would have been motivated to use a particular lipoxygenase recognized in the art to be suitable for use in a method of bleaching a textile.
Regarding claim 6, Hage et al. discloses use of at least one additional enzyme (para. 78), wherein the enzyme is pectin lyase (see p. 17 lines 7-10 of WO 01/00768 A1 which is incorporated by reference by Hage et al. at para. 80).
Regarding claim 9, Hage et al. discloses a detergent composition comprising a lipoxygenase (Abstract, para. 57), one or more alkyl polyglycoside surfactants (para. 70-73) (reads on one or more plant based biosurfactants, consistent with Applicant’s specification), and a lipase (para. 60-68).
Hage et al. is silent as to the composition comprising one or more polyunsaturated fatty acids.
However, Hage et al. discloses that it was known in the art to use an unsaturated fatty acid and lipoxygenase in solution in a process for bleaching a stain (para. 3).
Furthermore, Salmon et al. discloses that lipoxygenase activity during textile bleaching is enhanced by the addition of linoleic acid (reads on a polyunsaturated fatty acid) (para. 85-88, 208-210, 216-220).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the composition disclosed by Hage et al. to comprise linoleic acid (reads on one or more polyunsaturated fatty acids), based on the teachings of Salmon et al., in order to enhance the lipoxygenase activity during textile bleaching.
Regarding claim 11, Hage et al. discloses least one additional enzyme (para. 78), wherein the enzyme is pectin lyase (see p. 17 lines 7-10 of WO 01/00768 A1 which is incorporated by reference by Hage et al. at para. 80).
Regarding claim 14, Hage et al. discloses a method for bleaching a stain on a textile (para. 10-15, 21) comprising contacting the stain with a detergent composition in a wash liquor (para. 21, 90-95), the detergent composition comprising a lipoxygenase (Abstract, para. 57), one or more alkyl polyglycoside surfactants (para. 70-73) (reads on one or more plant based biosurfactants, consistent with Applicant’s specification), and a lipase (para. 60-68).
Hage et al. is silent as to the particular range of about 0.1-2.0 g detergent/L wash liquor, and is silent as to the composition comprising one or more polyunsaturated fatty acids.
As to the limitation regarding the range amount of detergent in the wash liquor, it has been held that where 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, when the particular parameter is recognized as a result-effective variable (MPEP §2144.05). Hage et al. discloses general conditions for the grams of detergent per liter of wash liquor (para. 90-95), and the skilled artisan would clearly recognize the amount of detergent per liter of wash liquor as a result-effective variable, as this parameter would affect the cleaning activity as is notoriously well known in the art. Therefore, it would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to discover an optimum or workable range by routine experimentation.
As to the limitation regarding the one or more polyunsaturated fatty acids, Hage et al. discloses that it was known in the art to use an unsaturated fatty acid and lipoxygenase in solution in a process for bleaching a stain (para. 3).
Furthermore, Salmon et al. discloses that lipoxygenase activity during textile bleaching is enhanced by the addition of linoleic acid (reads on a polyunsaturated fatty acid) (para. 85-88, 208-210, 216-220).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the composition disclosed by Hage et al. to comprise linoleic acid (reads on one or more polyunsaturated fatty acids), based on the teachings of Salmon et al., in order to enhance the lipoxygenase activity during textile bleaching.
Regarding claim 15, Hage et al. discloses wherein the contacting is performed under wash conditions (para. 21, 90-95).
Regarding claim 16, Hage et al. discloses wherein the one or more polyunsaturated fatty acids comprises linoleic acid, as set forth in the rejection of claim 1, above.
Regarding claim 19, Hage et al. discloses wherein the biosurfactant is alkyl polyglycoside (APG), as set forth in the rejection of claim 9, above.
Claims 5, 10, 17 and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Hage et al. (US Patent Application Publication 2003/0166485) (already of record) in view of Salmon et al. (US Patent Application Publication 2006/0042020) (already of record), as applied to claims 1 and 9, respectively, and in further view of Callisen et al. (WO 2014090940 A1) (already of record).
Regarding claim 5, Hage et al. discloses the polypeptide having lipoxygenase activity, as set forth above.
Hage et al. is silent as to the polypeptide having lipoxygenase activity has at least 60% sequence identity to the polypeptide of SEQ ID NO: 1.
However, Callisen et al. discloses that it was known in the art to use a lipoxygenase having 100% sequence identity to the polypeptide of SEQ ID NO: 1 when bleaching or removing a stain from a textile owing to the ability of this lipoxygenase to catalyze the oxygenation of polyunsaturated fatty acids (p. 2 lines 6-27, p. 13 lines 9-29; SEQ ID NO: 3 disclosed by Callisen et al. has 100% sequence identity to the polypeptide of SEQ ID NO: 1, as discussed in pp. 5-7 of the prior Non-Final Rejection dated 11/24/2025 and as stated in Applicant’s own specification as-filed). Callisen et al. discloses that the lipoxygenase “preferably” has the aforementioned sequence (p. 13 lines 27-29).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the method disclosed by Hage et al. such that the lipoxygenase has the sequence of SEQ ID NO: 3 disclosed by Callisen et al. (100% sequence identity to the polypeptide of SEQ ID NO: 1; falls within the claim range), as Callisen et al. discloses that such a lipoxygenase is “preferably” used in a method for bleaching or removing a stain on a textile, and the skilled artisan would have been motivated to use a particular lipoxygenase having an identity recognized in the art to be preferred in this process. In any case, substitution of one known lipoxygenase for another represents a simple substitution of one known element for another to obtain predictable results, in this case, the predictable result of achieving bleaching a stain on a textile.
Regarding claim 10, Hage et al. discloses the lipoxygenase, as set forth above.
Hage et al. is silent as to wherein the lipoxygenase has at least 60% sequence identity to the polypeptide of SEQ ID NO: 1.
However, Callisen et al. discloses that it was known in the art to use a lipoxygenase having 100% sequence identity to the polypeptide of SEQ ID NO: 1 when bleaching or removing a stain from a textile owing to the ability of this lipoxygenase to catalyze the oxygenation of polyunsaturated fatty acids (p. 2 lines 6-27, p. 13 lines 9-29; SEQ ID NO: 3 disclosed by Callisen et al. has 100% sequence identity to the polypeptide of SEQ ID NO: 1, as discussed in pp. 5-7 of the prior Non-Final Rejection dated 11/24/2025 and as stated in Applicant’s own specification as-filed). Callisen et al. discloses that the lipoxygenase “preferably” has the aforementioned sequence (p. 13 lines 27-29).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the method disclosed by Hage et al. such that the lipoxygenase has the sequence of SEQ ID NO: 3 disclosed by Callisen et al. (100% sequence identity to the polypeptide of SEQ ID NO: 1; falls within the claim range), as Callisen et al. discloses that such a lipoxygenase is “preferably” used in a method for bleaching or removing a stain on a textile, and the skilled artisan would have been motivated to use a particular lipoxygenase having an identity recognized in the art to be preferred in this process. In any case, substitution of one known lipoxygenase for another represents a simple substitution of one known element for another to obtain predictable results, in this case, the predictable result of achieving bleaching a stain on a textile.
Regarding claim 17, Hage et al. in view of Callisen et al. teaches wherein the polypeptide having lipoxygenase activity has 100% sequence identity to the polypeptide of SEQ ID NO: 1 (falls within the claim range), as set forth in the rejection of claim 5, above.
Regarding claim 20, Hage et al. in view of Callisen et al. teaches wherein the polypeptide having lipoxygenase activity has 100% sequence identity to the polypeptide of SEQ ID NO: 1 (falls within the claim range), as set forth in the rejection of claim 10, above.
Claims 8, 12, 18, and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Hage et al. (US Patent Application Publication 2003/0166485) (already of record) in view of Salmon et al. (US Patent Application Publication 2006/0042020) (already of record), as applied to claims 1 and 9, respectively, and in further view of Hansen et al. (US Patent Application Publication 2017/0306269; publication of US 15/513435).
Regarding claim 8, Hage et al. discloses the lipase, as set forth above.
Hage et al. is silent as to wherein the lipase has at least 60% sequence identity to the polypeptide of SEQ ID NO: 2.
Hansen et al. discloses a method of removing a stain from a textile comprising contacting the textile with a lipase (para. 447-450). Hansen et al. discloses that it is desirable to minimize development of odors when using lipase to treat textiles (para. 3). Hansen et al. discloses that a lipase having at least 90% but less than 100% sequence identity to the polypeptide they term “SEQ ID NO: 2” is effective for removing stains from textile while having the benefit of reduced odor development (Abstract, para. 69, 450). The polypeptide termed “SEQ ID NO: 2” of Hansen et al. is 100% identical to SEQ ID NO: 2 of the instant application (see ABSS search result below).
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It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the lipase disclosed by Hage et al. to have at least 90% but less than 100% (falls within the claim range) sequence identity to the polypeptide of SEQ ID NO: 2, as Hansen et al. discloses that such a lipase is effective for removing stains from textiles while providing the benefit of reduced odor development, and the skilled artisan would have been motivated to suppress odor development during textile treating. In any case, substitution of one known lipase for another represents a simple substitution of one known element for another to obtain predictable results, in this case, the predictable result of achieving stain removal from a textile.
Regarding claim 12, Hage et al. discloses the lipase, as set forth above.
Hage et al. is silent as to wherein the lipase has at least 60% sequence identity to the polypeptide of SEQ ID NO: 2.
Hansen et al. discloses a method of removing a stain from a textile comprising contacting the textile with a lipase (para. 447-450). Hansen et al. discloses that it is desirable to minimize development of odors when using lipase to treat textiles (para. 3). Hansen et al. discloses that a lipase having at least 90% but less than 100% sequence identity to the polypeptide they term “SEQ ID NO: 2” is effective for removing stains from textile while having the benefit of reduced odor development (Abstract, para. 69, 450). The polypeptide termed “SEQ ID NO: 2” of Hansen et al. is 100% identical to SEQ ID NO: 2 of the instant application (see ABSS search result presented in the rejection of claim 6, above).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the lipase disclosed by Hage et al. to have at least 90% but less than 100% (falls within the claim range) sequence identity to the polypeptide of SEQ ID NO: 2, as Hansen et al. discloses that such a lipase is effective for removing stains from textiles while providing the benefit of reduced odor development, and the skilled artisan would have been motivated to suppress odor development during textile treating. In any case, substitution of one known lipase for another represents a simple substitution of one known element for another to obtain predictable results, in this case, the predictable result of achieving stain removal from a textile.
Regarding claim 18, Hage et al. discloses the lipase, as set forth above.
Hage et al. is silent as to wherein the lipase has sequence identity to the polypeptide of SEQ ID NO: 2 within a range as set forth in claim 18.
Hansen et al. discloses a method of removing a stain from a textile comprising contacting the textile with a lipase (para. 447-450). Hansen et al. discloses that it is desirable to minimize development of odors when using lipase to treat textiles (para. 3). Hansen et al. discloses that a lipase having at least 90% but less than 100% sequence identity to the polypeptide they term “SEQ ID NO: 2” is effective for removing stains from textile while having the benefit of reduced odor development (Abstract, para. 69, 450). The polypeptide termed “SEQ ID NO: 2” of Hansen et al. is 100% identical to SEQ ID NO: 2 of the instant application (see ABSS search result presented in the rejection of claim 6, above).
It would have been obvious to one of ordinary skill in the art at the time before the effective filing date of the claimed invention to modify the lipase disclosed by Hage et al. to have at least 90% but less than 100% (falls within the claim range) sequence identity to the polypeptide of SEQ ID NO: 2, as Hansen et al. discloses that such a lipase is effective for removing stains from textiles while providing the benefit of reduced odor development, and the skilled artisan would have been motivated to suppress odor development during textile treating. In any case, substitution of one known lipase for another represents a simple substitution of one known element for another to obtain predictable results, in this case, the predictable result of achieving stain removal from a textile.
Regarding claim 21, Hage et al. in view of Hansen et al. teaches wherein the lipase has at least 90% but less than 100% (falls within the claim range) sequence identity to the polypeptide of SEQ ID NO: 2, as set forth in the rejection of claim 12, above.
Conclusion
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/HOLLY KIPOUROS/Primary Examiner, Art Unit 1799
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