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 .
DETAILED ACTION
2. Examiner has considered Patent Board Decision (5/12/2026) and latest filed claim filed on 6/10/2026. Accordingly, a new ground of rejection has been made in this office action. The action is made as non-final.
Status of the application
3. Claims 1, 6-12, 20-28, 36-64, 99-103 are pending in this office action.
Claims 36-64 have been withdrawn.
Claims 13-19, 29-35, 65-67, 68-98 have been cancelled.
Claims 1, 6-12, 20-28, 99-103 have been rejected.
Claim Rejections - 35 USC § 112
4. 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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
5. Claims 1, 6-12, 20-28, 99-103 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites “wherein said contacting is performed at a temperature of 55 degree C or more”. This clarifies that the ‘process which includes ‘contacting’ step, is performed at 55 degree C or more” as was raised by the board (BPAI decision 5/12/2026, sixth page , last paragraph). However, it is also to be noted that 55 degree C or more can be any temperature higher than 55 -degree C. The enzyme has its activity at a certain temperature range and within this range of temperature, if in contact with lactose containing substrate, it will exhibit its activity. Otherwise, as claim 1 claims any temperature, above, 55 degree C, it can be as high temperature where, lactase enzyme will be inactivated and without any enzyme activity. Therefore, it is suggested to have a temperature range at which the process including ‘contacting’ between lactose (containing substrate) and enzyme lactase will be performed.
Claim Rejections - 35 USC § 103
6. The following is a quotation of 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
6a. —_ In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AlA) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102 of this title, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negatived by the manner in which the invention was made.
6b. The factual enquiries set forth in Graham v. John Deere Co., 383 U.S. 1,148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S. C. 103(a) are summarized as follows:
a. Determining the scope and contents of the prior art.
b. Ascertaining the differences between the prior art and the claims at issue.
c. Resolving the level of ordinary skill in the pertinent art.
d. Considering objective evidence present in the application indicating obviousness or non-obviousness.
7. Claims 1, 6-21, 22, 23-35, 68, 99, 100, 101, 102, 103 are rejected under 35 U.S.C. 103(a) as being unpatentable over Hendriksen et al. US 2018/0295846 in view of Larsen et al. (WO 2017/106274 A1) and as evidenced by NPL amino acid abbreviation and as evidenced by NPL SEQ alignment Search Result (page 1) and as evidenced by NPL Milk sugar lactose.
8. Regarding claims 1, 6, 12, 23, 99 and 102, Hendriksen et al. discloses a method for reducing lactose in a milk-based substrate containing lactose in order to produce a low lactose fermented dairy product (at least in [0027]). Hendriksen et al. also discloses that the fermentation can be carried out with a lactase producing microorganism ([0030]) which can include Lactobacillus delbrueckii bulgaricus ([0045], [(0079], [0030]-[0031]) at a temperature of at least 55 degree C (at least in [0020], [0021], [0031]) or the substrate containing lactose can be treated with the enzyme lactase also (at least on [0119], [0120]) and wherein said lactose reduces the amount of lactose in said substrate by at least about 70% (at least in [0035]). Hendriksen et al. also discloses that milk-based substrate ([0010], [0012], [0020], [0079]) and it includes broadly a dairy product including whole milk, skim milk, etc. ([0059], [0060]) and it can be preferred raw milk also ([0143], [0144]). Hendriksen et al. also discloses that lactase enzyme can be used directly also (at least in [0020]).
Hendriksen et al. discloses that the origin of the enzyme can be from many sources including Lactobacillus delbrueckii bulgaricus ([0076], [0079]) and is active at about 55 degree C ([006)). Hendriksen et al. discloses pH optimum is above pH 5.0 (at least in [0025]) which is applicable for a broad source of lactase enzyme source (at least in ([0045], [0079]) [O030]- [0031]). It is to be noted that and as evidenced by applicant's specification that the lactase enzyme from Lactobacillus delbrueckii bulgaricus having neutral lactase activity.
However, Hendriksen et al. is specifically silent about (i) “neutral lactase” activity” and (ii) wherein said enzyme has at least 95,96,97,98,99 or 100% sequence identity to SEQ ID No 1”as claimed in claim 1.
With respect to (i) and (ii), Larsen et al. discloses the method to derive the pure enzyme from Lactobacillus delbrueckii bulgaricus having neutral lactase activity having pH optima 6.0-7.5 which is a choice for specific application like applications to treat foods like milk, ice cream whey, cheese etc. (at least on page 3 lines 7-11, even if in background section, it is all prior known fact). Larsen et al. discloses that Lactobacillus delbrueckii bulgaricus can be intracellular produced lactase (page 5 lines 30-32) and it is known that intracellular derived lactase has higher Neutral pH (page 3 lines 9-10).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Hendriksen et al. to include the teaching of Larsen et al. to consider to derive pure intracellular derived lactase from Lactobacillus delbrueckii bulgaricus which is neutral lactase for specific application (at least in Larsen et al. page 3 lines 3-1 and page 5 lines 30-32).
9. Regarding claim 1 and claim 6, it is to be noted that and as disclosed by Larsen et al. that the L. delbrueckii bulgaricus lactase Sequence was publicly available as UNIPORTKB - POC1Y0 (BGAL_ LACDE) (www.uniport .org /uniport/POC1Y0) which is SEQ ID # 1 (page 6) and it also matches at least about 100% identical with the amino acid seq of L. bulgaricus lactase (page 6 lines 3-35) with the claimed SEQ ID #1 which meets “at least 100% identity to SEQ ID No 1 of claim 1. It is to be noted that the disclosed SEQ ID #1 (in Larsen, page 6 e.g. SEQ ID #1 starts with MSNKL... are the abbreviated known symbols of the respective amino acids) which matches with claimed SEQ ID #1 (e.g., in PGPUB SEQ ID #1 starts with Met Ser Asn Lys and the symbols stands for MSNKL etc. as is known and is also evidenced by NPL amino acid abbreviation) that disclosed SEQ ID #1 is 100% identical to the claimed sequence ID NO 1 of amended independent claim 1 and is also further evidenced from NPL SEQ alignment search result (page 1, Query Match is 99.9%).
It is also to be noted that even if claim 1 does not recite the source of lactase enzyme is from Lactobacillus delbrueckii, however, it is evidenced that claimed SEQ ID No 1 (from cancelled claims 2-4, evidenced from applicants’ specification) is from Lactobacillus delbrueckii. Therefore, the disclosed enzyme having identical source and having ‘at least 100 % identical sequence’ with claimed SEQ ID No 1 will have identical claimed enzymatic property to have lactose reduction by at least 70% at about 55-degree C. Also, it meets the claim limitation of claim 6.
10. Regarding claims 1, 12, and 99, regarding the claim limitation of “wherein said contacting is performed at a temperature of “55 degree C or more” as claimed in amended claim 1 and “ 65 degree C or less (i.e. 55-65 degree C) as claimed in claim 12 and “at about 55-60 degree C as claimed in claim 99, Hendriksen et al. discloses that lactase enzyme can be used directly also (at least in [0020]) and also the substrate containing lactose can be treated with the enzyme lactase also (at least on [0119], [0120]) at a temperature of at least 55 degree C (at least in [0020], [0021], [0031]) which means “contacting is performed” between “substrate and enzyme” in order to achieve said lactose reduction in said lactose containing substrate by at least about 70% (at least in [0035]).
Larsen et al. discloses that the enzymatic activity is in the range of temperature from 10-70 degree C (Page 7 lines 17-20).
It is also to be noted that even if claim 1 does not recite the source of lactase enzyme is from Lactobacillus delbrueckii, however, it is evidenced from the applicant’s specification that the claimed SEQ ID No 1 is from Lactobacillus delbrueckii. Therefore, as discussed above that Larsen et al. discloses specifically SEQ ID No 1 is the sequence of Lactobacillus delbrueckii (at least SEQ ID #1, page 6) which has at least 100 % identical sequence with claimed SEQ ID No 1 and claimed SEQ ID No 1 is also from Lactobacillus delbrueckii, therefore, it will have identical claimed enzymatic property to have “lactose reduction by at least about 95%” under the condition of “wherein said contacting is performed at a temperature of 55 degree C or more” as claimed in claim 1 and also 65 degree C or less (i.e. 55-65 degree C) as claimed in claim 12 which depends on claim 1.
11. Regarding claims 1, 23, 102, Hendriksen discloses that the low-lactose milk product with longer shelf life can be made by using the disclosed method ([0137]- [0141]) and preferably less than 80% can be hydrolyzed and more than 90% hydrolyzed after one week (at least in [0147]). Therefore, it meets claim limitation of “at least 95-100%” reduction of lactose as claimed in amended claim 1 and “at least 96-100%” reduction of lactose claims 23, and “at least 97-100%” reduction of lactose as claimed in claim 102.
Absent showing of unexpected results, the specific amount of lactase reduction is not considered to confer patentability to the claims. As the lactose hydrolysis (and therefore, lactose reduction) is variable that can be modified, among others, by adjusting the amount of lactase enzyme, and time of hydrolysis, the precise degree of hydrolysis would have been considered a result effective variable by one having ordinary skill in the art at the time the invention was made. As such, without showing unexpected results, the claimed amount cannot be considered critical. Accordingly, one of ordinary skill in the art at the time the invention was made would have optimized, by routine experimentation, the amount of lactose reduction in Hendriksen et al., to
amounts, including that presently claimed, in order to obtain the desired effect e.g., desired amount of lactose reduction (In re Boesch, 617 F.2d. 272, 205 USPQ 215 (CCPA 1980)), since it has been held that where the general conditions of the claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. (In re Aller, 105 USPQ 223).
12. Regarding the amended claim limitation of “by at least about 95% within 180 minutes” as claimed in amended claim 1, it is also to be noted that this is variable and depends on the desired degree of hydrolysis to obtain final hydrolyze product containing the desired amount of residual (nil) lactose (substrate) after the enzyme lactase treatment. one of ordinary skill in the art would consider to optimize the enzyme mediated reduction of the amount of lactose in said substrate by at least about 95% within 180 minutes” as claimed in amended claim 1.
Absent showing of unexpected results, the specific amount of time is not considered to confer patentability to the claims. As the degree of hydrolysis are variables that can be modified, among others, by adjusting the amount of time the lactase enzyme needs depends on a particular temperature at which enzyme mediated reduction of lactose is performed, with the particular strength and amount of lactase enzyme, the precise amount would have been considered a result effective variable by one having ordinary skill in the art at the time the invention was made. As such, without showing unexpected results, the claimed amount cannot be considered critical. Accordingly, one of ordinary skill in the art at the time the invention was made would have optimized, by routine experimentation, the amount of time at a particular temperature in Hendriksen et al., to amounts, including that presently claimed, in order to obtain the
desired effect e.g., desired reduction of the amount of lactose in said substrate by at least about 95% within 180 minutes” (In re Boesch, 617 F.2d. 272, 205 USPQ 215 (CCPA 1980)), since it has been held that where the general conditions of the claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. (In re Aller, 105 USPQ 223).
It is also to be noted that Hendriksen and Larsen discloses identical lactase enzyme and its source as claimed in the claimed invention, therefore, the property of the enzyme will remain identical including the claimed property of “reduction of lactose by at least about 95% within 180 minutes” to the claimed property as claimed in amended claim 1 .
13. Regarding claims 7-11, Hendriksen et al. discloses that the lactase can be purified to make it at least 90% pure form ([0166]) and purification can be broadly performed by using unit operations like filtration, precipitation and chromatography ([(0165]) and/or recombinantly produced in order to make pure with minor/nil other proteins being present ([0166]).
Larsen et al. discloses specifically one isoelectric precipitation method to precipitate lactase from Lactobacillus delbrueckii bulgaricus which makes pure enzyme (protein) and eliminates all contaminants.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Hendriksen et al. to include the teaching of Larsen to perform purification of specific lactase enzyme having disclosed SEQ ID #1 which is lactase from L. delbrueckii bulgaricus lactase by isoelectric precipitation method to make pure lactase enzyme. It is to be noted that the isoelectric precipitated lactase is considered as concentrated form to meet claim 8.
It is also to be noted that the combined teaching method discloses few methods to purify including isoelectric precipitation to specifically precipitate claimed lactase which would have obvious reduced level of lipase as claimed in claim 9 and other enzymes as claimed in claims 10, 11. It is also to be noted that one of ordinary skill in the art may make recombinant construct by using the SEQ | D # 1 from Larson et al. to modify Hendriksen’s recombinant lactase (in Hendriksen et al. [0166]) for producing specific recombinant lactase from L. delbrueckii bulgaricus which makes recombinantly produced single enzyme protein free from all claimed elements as claimed in claims 9-11.
14. Regarding claims 20, Hendriksen et al. discloses milk-based substrate ((0010], [0012], [0020], [0079]), and it includes broadly a dairy product including whole milk, skim milk, etc. ([(0059], [0060]) and it can be preferred raw milk also ([0143], [0144)]). Hendriksen et al. also discloses that the dairy product can be condensed milk also (at least in [0005], [0060], [0067], [0112]). Hendriksen et al. also discloses that the dairy product can be pasteurized milk to eliminate or to reduce contamination of harmful microorganisms ([0056], [0058], [0143], [0229]), and it can be UHT milk (i.e., pasteurized) ([0060], [0112]).
15. Regarding claim 21, in addition to what is mentioned for claim 20 above, it would also have been obvious that one of ordinary skill in the art would have been motivated to perform the step of pasteurization after the “contacting step” with said enzyme with a reasonable expectation of success to have pasteurized enzyme treated lactose reduced (minimal) final product in order to eliminate or to reduce contamination of harmful microorganisms ([0056], [0058], [0143], [0229]) from the final product.
16. Regarding claims 22, 100, 101, it is known and Hendriksen et al. also discloses that milk has 5% lactose ([0192], [0195]). It is also evidenced by NPL Milk Sugar lactose that whole milk has 5% lactose (Page 1).
17. Regarding claims 24, 25, 26, 103, it is to be noted that and as mentioned for claim 23, the hydrolysis can make residual minimal/nil lactose in the final product which includes ppm level of residual lactose as claimed in claim 24, It is within the skill of one of ordinary skill in the art before the effective filling date of the claimed invention to optimize the hydrolysis condition by varying the time and temperature or by varying the time at a particular temperature as claimed in claim 25 with a desired concentration of enzyme (NLU lactase enzyme per gm lactose) as claimed in claim 26 in order to achieve most/all lactose hydrolysis, leaving minimal/nil lactose in the final product.
Absent showing of unexpected results, the specific amount of time is not considered to confer patentability to the claims. As the degree of hydrolysis are variables that can be modified, among others, by adjusting the amount of time and at a particular temperature (e.g., 37 degree C as claimed in claim 18) and using a desired concentration of the lactase enzyme, the precise amount would have been considered a result effective variable by one having ordinary skill in the art at the time the invention was made. As such, without showing unexpected results, the claimed amount cannot be considered critical. Accordingly, one of ordinary skill in the art at the time the invention was made would have optimized, by routine experimentation, the amount of time at a particular temperature 37 degree C in Hendriksen et al., to amounts, including that presently claimed, in order to obtain the desired effect e.g., taste, texture etc. (In re Boesch, 617 F.2d. 272, 205 USPQ 215 (CCPA 1980)), since it has been held that where the general conditions of the claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. (In re Aller, 105 USPQ 223).
18. Regarding claims 27, 28, Hendriksen et al. discloses that the disclosed invention provides lactase enzyme having very low transgalactosylating activity (see [[0010]) and having more than 1:1 ratio (at least in [0179]). It is also to be noted that and it is obvious that the disclosed method using the disclosed specific source and enzyme are identical to the claimed method, with the claimed source and claimed structure of the lactase enzyme, therefore, disclosed enzyme would have identical property including “lactose: transgalactosylase activity of more than 1:1, as claimed in claim 27 and “wherein said enzyme has a ratio of lactase activity above 100%” as claimed in claim 28.
Response to Arguments
19. Applicant’s prior arguments and response to arguments made in the prior mailed Examiner’s Answer to appeal brief ( 11/17/2025) are considered and is applicable here too. In addition, BPAI decision (5/12/2026) is discussed below.
(a) It is to be noted that BPAI (Patent Board Decision posted on 5/12/2026) has mentioned that “Thus, contrary to Appellant’s arguments , Hendriksen et al. does not teach away” and also Hendriksen et al. and Larsen are combinable as presented with detailed explanation by the Board [SEE First paragraph on 10th page of patent board decision (i.e. BPAI Decision posted 5/12/2026)]. This is discussed with respect to claim 69 which is cancelled in the latest filed claims as filed on 6/10/2026. This is also applicable for amended claim 1. The reason is, even if claim 69 is cancelled, prior cancelled claim 69 and currently amended claim 1 share common claim limitation of “ an enzyme having neutral lactase activity wherein said enzyme has at least about 95, 96, 97, 98, 99 or 100% sequence identity to SEQ ID NO:1 as claimed in claim 1 and it was in the cancelled claim 69.
(b) BPAI has reversed the rejection of independent claim 1 based on the fact that and as mentioned on sixth page, second paragraph (BPAI posted 5/12/2026) that
Claim 1 recites contacting said substrate with an enzyme having neutral lactase activity” at a temperature of 55°C or more." Appeal Br. 9 (Claims App.). It is not clear from this claim language how the temperature is incorporated into the claimed method. It is not clear from this claim language whether the temperature refers to a property of the enzyme, that is, the enzyme having the property of having neutral lactase activity at a temperature of 55°C or more, or whether the process is performed at a temperature of 55°C or more. We also observe that "said lactase" recited in claim 1 lacks antecedent basis because the term preceded by ‘enzyme’ and ‘lactase activity’ rather than lactase in claim 1”. This renders claim 1 indefinite. Therefore, applicants further amended claim 1 and filed 6/10/2026 to overcome 112 second paragraph rejections as mentioned by the board as discussed above.
Upon review, Examiner noticed that the amendment of claim 1 as filed 6/10/2026 provides better clarity. It is also to be noted that the board (BPAI) mentioned that because “examiner and Board cannot interpret claim 1 the merits of the Examiner’s rejection becomes difficult to analyze under 103 obviousness rejection” (page 8, first paragraph, Under BPAI decision ). However, there is no further additional points mentioned by the board which overcomes the 103 obviousness rejections of record. Upon review, the independent claim 1 is still not clear as discussed under 112 second paragraph rejection above. However, as mentioned by the board that this lack of clarity makes an erroneous claim interpretation and becomes difficult to find differences between the prior arts of record and the claims , at least independent claim 1 (Under BPAI decision, seventh page). However, there is no further issues addressed for 103 obviousness rejection. Therefore, examiner maintained the 103- obviousness rejection using identical combinations of prior arts of record and considering latest filed claims as filed 6/10/2026. Therefore, the rejection is made with the prior combinations of prior arts of record.
The rejection is made as non-final.
Conclusion
20. Any inquiry concerning the communication or earlier communications from the examiner should be directed to Bhaskar Mukhopadhyay whose telephone number is (571)-270-1139.
If attempts to reach the examiner by telephone are unsuccessful, examiner’s supervisor Erik Kashnikow, can be reached on 571-270-3475. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/BHASKAR MUKHOPADHYAY/Examiner, Art Unit 1792
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