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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 10/27/2025 has been entered.
Withdrawal of Rejections
The response and amendments filed on 10/27/2025 are acknowledged. Any previously applied minor objections and/or minor rejections (i.e., formal matters), not explicitly restated here for brevity, have been withdrawn necessitated by Applicant’s formality corrections and/or amendments. For the purposes of clarity of the record, the reasons for the Examiner’s withdrawal, and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner’s Response to Arguments section.
Briefly, the previous 35 U.S.C. 112(b) rejection for indefiniteness has been withdrawn necessitated by Applicant’s amendment. The previous 35 U.S.C. 112(a) rejection for written description has been withdrawn necessitated by Applicant’s amendment. The previous 35 U.S.C. 102 rejection for anticipation in view of Cervin has been withdrawn; however, new grounds of rejection have been set forth below. The previous 35 U.S.C. 103 rejection for obviousness in view of Cervin, Lassen, Breneman, and Petkov has been withdrawn; however, new grounds of rejection have been set forth below.
The following rejections and/or objections are either reiterated or newly applied. They constitute the complete set presently being applied to the instant application.
New Grounds of Rejection Necessitated by Amendments
Claim Rejections - 35 USC § 102, Anticipation
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 1-2 and 14 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Lassen (US 2010/0083392; Date of Publication: April 1, 2010 – previously cited).
Lassen’s general disclosure relates to a phytase derived from Hafnia alvei that comprises modification in the amino acid sequence for improved properties, such as, protease stability, heat stability, steam stability, pelleting stability, and performance in animal feed (see, e.g., Lassen, abstract). More specifically, Lassen discloses that the variant phytases contain specific amino acid substitutions in order exhibit improved properties compared to the parent phytase (see, e.g., Lassen, [0022]-[0024]), wherein the improved properties are “Stability (such as acid-stability, heat-stability, steam stability, and/or protease stability, in particular pepsin stability), temperature profile, pH profile, specific activity, substrate specificity, performance in animal feed (such as an improved release and/or degradation of phytate), susceptibility to glycation, and/or glycosylation pattern. The phytase variants of the invention preferably exhibit improved properties in respect of thermal performance, such as heat-stability (temperature stability, thermostability), steam stability, pelleting stability and/or temperature profile; and/or protease stability, in particular pepsin stability, pH profile, specific activity, substrate specificity, performance in animal feed(such as an improved release and/or degradation of phytate), susceptibility to glycation, and/or glycosylation pattern” (see, e.g., Lassen, [0025]).
Regarding claim 1 pertaining to the engineered phytase polypeptide, the Examiner has interpreted this claim to be any polypeptide with any mutation that is recited within claim 1, wherein the position just needs to correspond to SEQ ID NO: 1, but not necessarily be SEQ ID NO: 1. Based on this, Lassen teaches a phytase polypeptide corresponding to SEQ ID NO: 2, wherein the phytase has a substitution at 45P and 314G (see, e.g., Lassen, [0030]).
Regarding claim 2 pertaining to the substitutions, Lassen teaches a phytase polypeptide that has a 234V substitution (see, e.g., Lassen, [0030]).
Regarding claim 14 pertaining to an animal feed composition, Lassen teaches that the phytase can be used within an animal feed composition and as an animal feed additive (see, e.g., Lassen, [0003]). Moreover, Lassen teaches Example 10, which shows the performance of the animal feed containing the phytase within an in vitro pig model (see, e.g., Lassen, Example 10). Additionally, Lassen teaches that the animal feed contains “maize, soybean meal and soybean oil as main constituents” along with the engineered phytases at suitable dosages (see, e.g., Lassen, [0367]).
Claim Rejections - 35 USC § 103, Obviousness
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Lassen as applied to claims 1-2 and 14 above, and further in view of Breneman (WO 2010/120471; Date of Publication: October 21, 2010 – previously cited).
The teachings of Lassen as it pertains to an engineered phytase polypeptide comprising amino acid substitutions that result in increased stability and improved properties is discussed above.
However, Lassen does not teach: wherein the phytase polypeptide has at least 90% sequence identity to SEQ ID NO: 1 (claim 3).
Breneman’s general disclosure relates to “processing grain/cereal starch into soluble dextrins and to ethanol without the addition of alkali or acid for pH adjustment” (see, e.g., Breneman, [002]). Additionally, Breneman discloses “a thermostable phytase, which avoids the need to adjust the pH of the grain/cereal slurry, obviates the need for low temperature phytase pretreatment, and allows liquefaction to proceed at unexpectedly high temperatures” (see, e.g., Breneman, [0016]).
Regarding claim 3 pertaining to a polypeptide or fragment thereof, Breneman teaches SEQ ID NO: 2 which has 100% sequence identity to SEQ ID NO:1 of the instant application (see, e.g., Breneman, Figure 4). Furthermore, Breneman teaches that SEQ ID NO: 2 is a thermostable phytase variant BP-17 from Buttiauxella sp. (see, e.g., Breneman, [0031]), wherein the BP17 phytase is “capable of hydrolyzing at least 50% of phytate present in a starch-containing grain slurry or mash (e.g., comprising about 32% DS) in about 20 minutes at a temperature of at least 80°C” (see, e.g., Breneman, [0068]).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Lassen’s engineered phytase polypeptide with the amino acid substitutions at positions 45, 314, and 234, wherein the phytase polypeptide has 100% sequence identity to Breneman’s SEQ ID NO: 2. One would have been motivated to do so because Breneman teaches that SEQ ID NO: 2 is a thermostable phytase variant BP-17 from Buttiauxella sp. (see, e.g., Breneman, [0031]), wherein the BP17 phytase is “capable of hydrolyzing at least 50% of phytate present in a starch-containing grain slurry or mash (e.g., comprising about 32% DS) in about 20 minutes at a temperature of at least 80°C” (see, e.g., Breneman, [0068]). Therefore, one would have been motivated to produce a variant phytase corresponding to Breneman’s SEQ ID NO: 2, wherein Breneman’s SEQ ID NO: 2 phytase polypeptide contains a 45P, 314G, and/or 234V amino acid substitution, as taught by Lassen, because Breneman teaches that SEQ ID NO: 2 is encodes a thermostable phytase and Lassen teaches that these amino acid substitutions within phytases result in improved thermostability (see, e.g., Lassen, abstract, [0030]-[0033]). Furthermore, based on the teachings of Lassen and Breneman, one of ordinary skill in the art would expect that a variant phytase corresponding to Breneman’s SEQ ID NO: 2, and wherein the variant also contains the 45P, 314G, and/or 234V amino acid substitutions, to have an additive effect compared to the parent phytase because both SEQ ID NO: 2 and the 45P, 314G, and/or 234V amino acid substitutions are known to enhance thermostability. These additive effects are further motivation for someone of ordinary skill in the art to produce a phytase variant corresponding to Breneman’s SEQ ID NO: 2, and wherein SEQ ID NO: 2 comprises amino acid substitutions at specific locations known to enhance phytase performance and increase thermostability, such as the 45P, 314G, and/or 234V amino acid positions, as taught by Lassen. One would have expected success because Lassen and Breneman both teach engineered phytase polypeptides with enhanced thermostability.
Claim 31 is rejected under 35 U.S.C. 103 as being unpatentable over Lassen as applied to claims 1-2 and 14 above, in view of Petkov (US 2019/0069584; Date of Publication: March 7, 2019 – previously cited).
Petkov’s general disclosure relates to engineered phytase enzymes exhibiting high thermostability compared to commercially available phytases (see, e.g., Petkov, abstract). Furthermore, Petkov discloses an appA3C phytase, wherein variants of this phytase exhibit drastically improved thermostability compared to other tested phytases (see, e.g., Petkov, [0013]). The specific mutations within the appA3C phytase variant that resulted in improved thermostability were at amino acid positions 26, 84, 159, 181, 207, 233, 277, and 349 of Petkov’s SEQ ID NO: 1 (see, e.g., Petkov, [0013]).
Regarding claim 31 pertaining to the phytase concentration, Petkov teaches that phytases were added to feed preparations at a concentration of 500 g/ton in order to evaluate “performance parameters such as weight gain and bone mineralization as indication of phosphate incorporation” (see, e.g., Petkov, [0129]).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Lassen’s engineered phytase polypeptide, wherein the polypeptide is added to feed preparations at a concentration of 500 g/ton, as taught by Petkov. One would have been motivated to do so because Petkov teaches that administration of phytase(s) at 500 g/ton allows for evaluation of the effect of the variant phytase(s), with enhanced thermostability, broad pH optimum, and fast enzyme kinetics (see, e.g., Petkov, [0012]), on “performance parameters such as weight gain and bone mineralization as indication of phosphate incorporation” (see, e.g., Petkov, [0129]). Therefore, one would have been motivated to administer Lassen’s variant phytase containing the 45P, 314G, and/or 234V amino acid substitutions at 500 g/ton because Lassen’s variant phytase exhibits improved properties, such as, protease stability, heat stability, steam stability, pelleting stability, and performance in animal feed (see, e.g., Lassen, abstract). Moreover, based on the teachings of Lassen and Petkov, it would have been obvious to administer Lassen’s variant phytase containing the 45P, 314G, and/or 234V amino acid substitutions to the animal feed at a concentration of 500 g/ton, as taught by Petkov, in order to assess various parameters within animals, such as weight gain and bone mineralization as indication of phosphate incorporation” (see, e.g., Petkov, [0129]). Furthermore, one of ordinary skill in the art would recognize that administration of variant phytases with enhanced stability and performance would be beneficial in animal feeds, and compositions in general. One would have expected success because Lassen and Petkov both teach engineered phytase polypeptides with enhanced thermostability.
Claim 32 is rejected under 35 U.S.C. 103 as being unpatentable over Lassen as applied to claims 1-2 and 14 above, and further in view of Kim (US 2019/0216867; Date of Publication: July 18, 2019 – newly cited).
The teachings of Lassen as it pertains to an engineered phytase polypeptide comprising amino acid substitutions that result in increased stability and improved properties is discussed above.
However, Lassen does not teach: wherein the direct fed microbial comprises one or more of a Lactobacillus sp. or a Bifidobacterium sp. (claim 32).
Kim teaches a novel Lactobacillus salivarius CJLS1511 strain that is added to animal feed compositions (see, e.g., Kim, abstract). Moreover, Kim teaches “Lactobacillus sp. microorganism is lactic acid producing bacteria commonly found in intestinal tract in animals, and performs homofermentation or hetero-fermentation using dairy products and vegetables as its substrates. Lactobacillus sp. microorganism is known to maintain intestinal environment as acidic condition in animals, inhibit overgrowth of harmful bacteria such as E. coli and Clostridium, improves diarrhea and constipation in animals, and help vitamin synthesis, and decrease serum cholesterol level, and have anti-cancerous activity, etc.” (see, e.g., Kim, [0002]).
Regarding claim 32 pertaining to the addition of a Lactobacillus sp. to the animal feed composition, Kim teaches animal feed compositions comprising Lactobacillus salivarius CJLS1511 (see, e.g., Kim, abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Lassen’s animal feed composition comprising the engineered phytase polypeptide, wherein the animal feed composition also comprises a Lactobacillus sp., such as Lactobacillus salivarius CJLS1511, as taught by Kim. One would have been motivated to do so because Kim teaches “Lactobacillus sp. microorganism is lactic acid producing bacteria commonly found in intestinal tract in animals, and performs homofermentation or hetero-fermentation using dairy products and vegetables as its substrates. Lactobacillus sp. microorganism is known to maintain intestinal environment as acidic condition in animals, inhibit overgrowth of harmful bacteria such as E. coli and Clostridium, improves diarrhea and constipation in animals, and help vitamin synthesis, and decrease serum cholesterol level, and have anti-cancerous activity, etc.” (see, e.g., Kim, [0002]). Additionally, Kim teaches when evaluating the activity of digestive enzymes when Lactobacillus salivarius CJLS1511 is added, Kim shows that “Lactobacillus salivarius CJLS1511 had higher activity of digestive enzymes such as protease activity, phytase activity, cellulose degradation activity, and amylase activity than those of the Lactobacillus salivarius KCCM 40210 standard strain” (see, e.g., Kim, Table 7 & [0068]). Moreover, Lassen teaches that the phytase can be used within an animal feed composition and as an animal feed additive (see, e.g., Lassen, [0003]), and that the phytase can have 45P, 314G, and/or 234V amino acid substitutions are known to enhance thermostability and properties within the animal feed (see, e.g., Lassen, [0022], [0024], [0030]). Therefore, based on the teachings of Lassen and Kim, it would have been obvious to produce an animal feed composition comprising a phytase with enhance thermostability and properties, along with a Lactobacillus sp. One would have expected success because Lassen and Kim both teach production of animal feed compositions.
Examiner’s Response to Arguments
Applicant's arguments filed 10/27/2025 have been fully considered but they are not persuasive.
Regarding Applicant’s argument that deletion of the 228Y substitution in claim 1 renders claim 1 and all dependent claims novel (remarks, pages 6-7), this argument is not persuasive because, as discussed above, the Examiner has interpreted claim 1 to be any polypeptide with any mutation that is recited within claim 1, wherein the position just needs to correspond to SEQ ID NO: 1, but not necessarily be SEQ ID NO: 1. Based on this, Lassen teaches a phytase polypeptide corresponding to SEQ ID NO: 2, wherein the phytase has a substitution at 45P and 314G (see, e.g., Lassen, [0030]). Therefore, claim 1 is anticipated by Lassen.
Conclusion
Claims 1-3, 14, and 31-32 are rejected.
No claims are allowed.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 EST.
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/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653