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 § 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.
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.
Claims 1-15 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.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 1 step (c) recites the broad recitation “the lactose content in the milk-based product is at least 0.5% (w/w)”, and the claim also recites “preferably at least 1% (w/w)” which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims. Clarification and /or correction is required.
Similar issue with claim 4 step b), recites the broad recitation “is reached is at most 5 minutes”, and the claim also recites “at most 2 minutes, at most 1 minute.” which are the narrower statement of the range/limitation. Clarification and /or correction is required.
Similar issue with claim 5 recites the broad recitation “from addition of the enzyme until the heat-treated milk-based product has been cooled to a temperature of at most 40° C”, and the claim also recites “at most 35° C., most 30° C.” which are the narrower statement of the range/limitation. Clarification and /or correction is required.
In addition claim 5 also recited the broad recitation of time “at most 3.5 minutes”, and the claim also recites “at most 3 minutes, at most 2.5 minutes, at most 2 minutes or at most 1 minute” which are the narrower statements of the range/limitation. Clarification and /or correction is required.
Similar issue with claim 6 recites the broad recitation “wherein the milk-based substrate comprises 2-30% lactose (w/w).” and the claim also recites “2-17%, more preferably 4-5.5% lactose (w/w)” which are the narrower statements of the range/limitation. Clarification and /or correction is required.
Similar issue with claim 10 recites the broad recitation “milk-based substrate is cooled to at most 40° C.” and the claim also recites “at most 35° C., at most 30° C.” which are the narrower statement of the range/limitation. Clarification and /or correction is required.
In addition claim 10 also recited the broad recitation of time “within 5 minutes” in line 3, and the claim also recites “within 3 minutes, within 2 minutes, within 1 minute” in lines 3-4 which are the narrower statements of the range/limitation. Clarification and /or correction is required.
Similar issue with claim 12 recites the broad recitation “the enzyme retains at least 0.1% of its initial activity”, and the claim also recites “at least 0.5%, at least 1%, at least 2%, at least 10%, at least 50%, at least 80%, at least 90” in the same claim, which are the narrower statements of the range/limitation. Clarification and /or correction is required.
Similar issue with claim 14 recites the broad recitation “lactase activity has a temperature optimum of 30-60° C”, and the claim also recites lactase activity has a temperature optimum of 35-55° C” in the same claim, which are the narrower statements of the range/limitation. Clarification and /or correction is required.
Similar issue with claim 15 recites the broad recitation “lactase activity has a residual activity of at least 0.5%”, and the claim also recites lactase residual activity “at least 1%, at least 2%, at least 3%, at least 5%, at least 10%” in the same claim, which are the narrower statements of the range/limitation. Clarification and /or correction is required.
Claims 1, 4,-6, 10, 12, 14-15 above are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Claim 15 is also indefinite for the recitation of a process of calculating residual enzymatic activity “after incubation in skimmed milk having a lactose content of 4.7% at 90° C. for 30 seconds, at 140° C. for 5 seconds and at 70° C. for 30 seconds followed by cooling to 0-10° C. and subsequent incubation at 23° C. for 72 hours”. As recited skimmed milk having a lactose content of 4.7% is subjected to incubation before cooling and further incubation. The three distinct incubation periods “at 90° C. for 30 seconds” “at 140° C. for 5 seconds” and “at 70° C. for 30 seconds” followed by cooling and subsequent incubation at 23° C. for 72 hours “, as recited it is unclear whether this method of calculation of residual enzymatic activity requires all three incubation periods “at 90° C. for 30 seconds” “at 140° C. for 5 seconds” and “at 70° C. for 30 seconds” or the measurement/ calculation of the residual enzymatic activity to be performed by choosing one of these incubation temperature and time set.
Further, as recited claim 15 appears to be assessing the residual enzymatic property, and recites the enzyme by its functional features of residual activity after a heat treatment, but it is unclear for one of ordinary skill at the time of effective filing of the application as to which enzymes fulfill such requirement. Furthermore, there is no clear definition of "initial activity", further rendering it unclear which enzymes should be considered under the recitation of claim 15.It is further unclear as to how the method of claim 15 affects the milk product of claim 1. Claim 12 is also directed to residual enzyme activity and is unclear, how it relates to the product of claim 1 and/or further narrows the scope of the claim from which it depends.
Clarification and /or correction is required.
Claim Rejections - 35 USC § 103
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-AIA ) 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.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1, 2, 4-15 are rejected under 35 U.S.C. 103 as being unpatentable over Tossavainen et al., (US 20100215828 A1), hereinafter Tossavainen, in view of Raj et al (WO 2018189224 A1), hereinafter Raj.
Regarding claim 1, Tossavainen teaches a method of producing a lactose-reduced heat-treated milk-based product (Example 2; [0065]-[0067]) where Tossavainen teaches Lactose-Hydrolyzed UHT Milk) which comprises:
a) adding an enzyme having lactase activity ([0066] lactase) to a milk-based substrate comprising at least 2% lactose (w/w) (Table 3 lactose % is 4.65%),
b) after addition of the enzyme, performing a heat treatment of the milk-based substrate by holding said milk-based substrate at a holding temperature of at least 120° C. for a holding time of at least 1 second followed by cooling to produce a heat-treated milk-based product ([0066] where UHT treatment of milk is taught where performing a heat treatment of the milk-based substrate by holding said milk-based substrate at a holding temperature of at least 146°C for a holding time of 4 seconds followed by cooling to produce a heat-treated milk-based product) where the temperature and time of heating falls in the claimed range; and
c) storing the heat-treated milk-based product for at least 4 days at a temperature of at most 40° C (67 "room temperature", 4 days of storage is implicit for a UHT milk product),
wherein after step b) but before step c) the lactose content in the milk-based product is at least 0.5% (w/w), preferably at least 1% (w/w) (Table 3 where lactose % is 4.65%), and wherein after step c) the lactose content in the milk-based product is at most 0.2% (w/w), (Table 3 where lactose % is 0.5%).
Although Tossavainen does not explicitly disclose the order of UHT treatment and lactose content after step b) and after step c), as the method of Tossavainen shares exactly the same steps with the same technical features as described in claim 1 of the present application, it follows that the lactose content of the treated milk based product in the claimed range can be achieved following the method of Tossavainen. UHT temperature range, order of UHT step and lactose content after step b) and after step c) is well known in the art at the time of the effective filing date of the invention as taught by Raj. Prior art to Raj teaches a method of treating a lactose-containing dairy product with beta-galactosidase (Abstract, page 2, lines 5-10, page 3, lines 15-24 and claim 5), and further discloses that the step of adding the beta-galactosidase/lactase can be performed in conjunction with a step of ultra heat treatment (Page 23, lines 27-to page 24, line 2; page 24, lines 6-10 and 19-25 and claim 14). Raj also teaches the temperature for UHT and advantages of lactase enzymes having activity at higher temperatures “For the UHT treatment, the temperature is typically either around 135°C or around 140°C. It is highly wanted that the enzymes may have activity in the range of a temperature up to 140°C so that the enzyme may be added to raw milk before the UHT step” (page 7, 10-20). Regarding the reduction in lactose concentration after step c) the lactose content in the milk-based product is at most 0.2% (w/w), Raj teaches lactose concentration is reduced to less than about 0.1% or lower, such as to less than about 0.01% (claim 20). Therefore, the claimed method steps of making a lactose-reduced heat-treated milk-based product was known in the art at the time of effective filing date of the invention. It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to include the step of UHT treatment of milk-based product after adding lactase/ galactosidase and also treat with type of galactosidase /lactase that can tolerate heat treatment as is taught by Raj, and such enzyme is added to milk based product in a dosage and left for treating milk based product for duration to achieve the desired percent of lactose. The ordinary artisan would have been motivated to modify the sequence of UHT treatment based on the type of lactase enzymes having activity at higher temperatures (as taught by Raj on page 7, 10-20) and add said enzyme in an amount and for duration such that the milk based product after treatment has a desired lactic acid content at least based on the type of milk-based product and the intended consumer of the finished milk-based product.
Regarding claim 2, Tossavainen in view of Raj teaches a method of claim 1. Tossavainen does not specify the heat treatment is done after adding lactase or wherein step b) is performed immediately after step a) without a dedicated incubation step after step a) and before step b). However, application of heat treatment either before, after or in conjunction with lactase/ beta-galalctosidase enzyme addition was known in the art at the time of effective filing date of the invention (as taught by Raj, Page 23, lines 27-to page 24, line 2; page 24, lines 6-10 and 19-25 and claim 14). It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to perform the heating step b) without a dedicated incubation step after step a) and before step b). The ordinary artisan would have been motivated to modify Tossavainen at least for the purpose of achieving hydrolyzing the desired proportion of lactose present in the milk-based product. One of ordinary skill would be motivated to modify the process step of reducing or eliminating the incubation period with lactase based on the type of lactase/beta galactosidase and the process conditions including temperature, pH, duration of lactose hydrolysis.
Regarding claim 4, Tossavainen in view of Raj teaches the method of claim 1, wherein the time from addition of the enzyme until the holding temperature of step b) is reached is 4 seconds according to Tossavainen (Para 66) which falls in the claimed range of time of at most 5 minutes, at most 2 minutes, at most 1 minute. Also see rejection under 35 USC 112 (second paragraph).
Regarding claim 5, Tossavainen in view of Raj teaches the method of claim 1, wherein the time from addition of the enzyme until the heat-treated milk-based product has been cooled to a temperature of at most 40° C., at most 35° C., most 30° C., is at most 3.5 minutes at most 3 minutes, at most 2.5 minutes, at most 2 minutes or at most 1 minute (see para 66 and 89) where cooling after 4-5 seconds of UHT treatment is taught, which falls in the claimed range of time for cooling. Also see rejection under 35 USC 112 (second paragraph).
Regarding claim 6, Tossavainen in view of Raj teaches the method of claim 1, wherein the milk-based substrate comprises 2-30%, 2-17%, more preferably 4-5.5% lactose (w/w), (see para 66 and tables 3 and 4) where lactose % falls in the claimed range. Also see rejection under 35 USC 112 (second paragraph).
Regarding claim 7, Tossavainen in view of Raj teaches the method of claim 1, wherein the milk-based substrate is milk comprising 4-5.5% lactose (w/w), (see para 66 and tables 3 and 4) where lactose % falls in the claimed range.
Regarding claim 8, Tossavainen in view of Raj teaches the method of claim 1, wherein the heat treatment is an ESL treatment, an ultra-pasteurization or a UHT treatment, (see para 66 ) where UHT treatment is taught and UHT treat is also taught by Raj on page 7, lines 10-20.
Regarding claim 9, Tossavainen in view of Raj teaches the method of claim 1, wherein the heat treatment is a UHT treatment performed at a temperature of 128-132° C. for 25-35 seconds, at a temperature of 138-140° C. for 2-5 seconds or at a temperature of 144-146° C. for 1-2 seconds (see para 66 where UHT treatment temperature of 146.degree. C for 4 seconds is disclosed, also in para 42, Tossavainen teaches typical treatment of milk under UHT includes “treatment (e.g. milk at 138.degree. C., 2 to 4 s)”, where the UHT treatment temperature and duration falls in the claimed range of at least temperature of 138-140° C. for 2-5 seconds as claimed .
Regarding claim 10, Tossavainen in view of Raj teaches the method of claim 1, where after the holding time of step b), the milk-based substrate is cooled to at most 40° C. at most 35° C., at most 30° C., within 5 minutes, within 3 minutes, within 2 minutes, within 1 minute (see para 66 and 89) where cooling after UHT treatment is taught, which falls in the claimed range of time for cooling. Further regarding claim 10 the cooling features of cooling and storing the milk-based substrate to at most 40°C, which is implicitly included in claim 1. Also see rejection under 35 USC 112 (second paragraph).
Regarding claim 11, Tossavainen in view of Raj teaches the method of claim 1, wherein after step b) but before step c) the milk-based product is aseptically packed (see para 67 where the aseptic package before storing/ step c) is taught by Tossavainen).
Regarding claim 13, Tossavainen teaches a method of claim 1, wherein the enzyme having lactase activity , however, Tossavainen does not specify that the lactase comprises in its amino acid sequence the motif WTXXDY [I/L/R]GE[P/S/A] and also at least one of the motifs SR[W/Y/F]YSGSGX[Y/G]R and/or [L/V/I]X[L/V/I]PHD as instantly claimed. Raj on page 40, lines 11-30 teaches SEQ ID NO:34 comprises the peptide motif of "WTGFDYLGEP" (starting from position 592, see specifically lines 19-21), thereby fulfilling the requirement of claim 13. The enzyme of SEQ ID NO: 34 as taught by Raj is used as the reference enzyme was known in the art at the time of effective filing date of the invention. Therefore it would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to include lactase enzyme having the amino acid sequence with motif as claimed. The ordinary artisan would have been motivated to modify Tossavainen and include the lactase enzyme as taught by Raj by Sequence listing 34 at least for the purpose of utilizing an enzyme that possess the functional properties as desired, such as temperature and pH sensitivity of the lactase enzyme to make it easier and efficient to produce a desired reduced lactose milk-based product.
Regarding claim 14, Tossavainen teaches a method of claim 1, wherein the enzyme having lactase activity has a temperature optimum of 30-60° C., 35-55° C.( Para 66, lactase activity has a temperature of 37. degree.C. Tossavainen is silent regarding the temperature of 37.degree. C being optimal temperature but it was known to one of ordinary skill in the art before the effective filing date of the invention and was typical to add and perform enzymatic treatments at temperature and acidity ranges that are close to optimal temperatures and pH conditions for an enzyme at least in order to achieve a desired enzymatic effect most economically and easily. Further, Raj teaches in background information that typical lactases were known to have temperature optimum around 37.degree.C (Page 1, lines 20-25).
At the time of the effective filing date of the invention it was known that
Tossavainen teaches enzyme treatment at 37.degree. C, which is in the claimed temperature range.
Typical lactases were known to have temperature optimum around 37.degree.C (Page 1, lines 20-25), which falls in the claimed range;
lactase enzymes having optimal treatment ranging from 25-140.degree.C (Page 23line 27-page 24, line 2 Raj)
enzymatic treatments are routinely performed near the optimal temperature and pH conditions for said enzymes as enzymes perform better near the optimal temperature for an enzyme, and
Therefore, in light of the knowledge available to one of ordinary skill in the art at the time of effective filing date of the invention and also in view of teaching provided by Raj, it would have been obvious to one of ordinary skill in the art that typical lactase enzyme or lactase as taught by as taught in para 66 of Tossavainen will have optimal temperature near the treatment temperature of 37. degree.C, i.e., the claimed range of the treatment. The ordinary artisan would have been motivated to modify utilize a lactase enzyme having the optimum temperature in a desired temperature range, such as 37. degree.C., at least for the purpose of performing the enzymatic reaction under cost effective and economical means.
Regarding claims 12 and 15, Tossavainen in view of Raj teach the method of claim 1, however, Tossavainen teaches incubation and skim milk with lactose content overlapping the range as claimed but does not specify recitation of claim 12 “wherein after step b), the enzyme retains at least 0.1% of its initial activity, at least 0.5%, at least 1%, at least 2%, at least 10%, at least 50%, at least 80%, at least 90%” and similar recitation of claim 15 is also related to residual enzyme activity of “at least 0.5%, at least 1%, at least 2%, at least 10%” followed by variations of incubation periods of “ 90° C. for 30 seconds, at 140° C. for 5 seconds and at 70° C. for 30 seconds followed by cooling to 0-10° C. and subsequent incubation at 23° C. for 72 hours”.
Given that the method steps of claim 1 taught by Tossavainen in view of Raj is substantially similar and the enzyme taught by applied art is also substantially the same as the claimed enzyme, and it follows that the enzyme activity before and also be substantially similar. As the enzyme of SEQ ID NO:34 in Raj comprises the peptide motif defined in claim 13, it should also have the same thermal resistance as in claims 12 and 15.
In the instant case The recitation of “the enzyme retains at least 0.1% of its initial activity, at least 0.5%, at least 1%, at least 2%, at least 10%, at least 50%, at least 80%, at least 90%” (claim 12) and similar recitation of enzyme retains “at least 0.5%, at least 1%, at least 2%, at least 10%” (claim 15) is only a statement of the inherent properties of the enzyme and its properties under various reaction times and temperatures. The enzyme recited in Tossavainen as well as Raj is substantially identical to that of the claims. 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, 195 USPQ 430, 433 (CCPA 1977) and MPEP 2112.01.
Regarding the incubation periods of claim 15, i.e., “after incubation in skimmed milk having a lactose content of 4.7% at 90° C. for 30 seconds, at 140° C. for 5 seconds and at 70° C. for 30 seconds followed by cooling to 0-10° C. and subsequent incubation at 23° C. for 72 hours” see rejection under 35 USC 112 (second paragraph). As Tossavainen in view of Raj teach the specific type of enzyme as claimed and Raj in particular teaches enzyme of SEQ ID NO:34 in Raj comprises the peptide motif defined in claim 13, it should facilitate lactose breakdown in the same way and have substantially same thermal resistance when subjected to various incubation periods separately or in succession followed by heat treatment as recited in claims 12 and 15.
Also see rejection under 35 USC 112 (second paragraph).
It is further noted that applicant has described the product with parameters and equations which cannot be measured by the office for prior art comparison, because the office is not equipped to manufacture prior art products and compare them for patentability purposes. Therefore, as a prima facia case of obviousness has been properly established, the burden is shifted to the applicant to show that the prior art product is different.
Also see rejection under 35 USC 112 (second paragraph).
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Tossavainen and Raj as applied to claim 1 above, further in view of Riis et al., (US 20190142022 A1), hereinafter Riis.
Regarding claim 3, Tossavainen in view of Raj teaches method claim 1, wherein pumping equipment has been fitted to add the enzyme to the milk-based substrate while said milk-based substrate is streaming through process equipment, such as process pipes (see para 66 of Tossavainen where “and pumped into a sterile tank after cooling to 10.degree. C. (milk base). The lactase treated lactose fraction was run through the same UHT process and added to the above milk base”. As Tossavainen teaches pump and tank that are typical milk processing equipment, Tossavainen is silent about in line dosing. However, milk processing plants having in line dosing options were known in the art at the time of the invention as taught by Riis where “lactase is added to the acidified milk product by in-line dosing into a pipe, and subsequently the lactase is mixed into the yogurt in the pipe by a mixing device. Preferably, the mixing device is selected from the group consisting of at least one bend of the pipe, a back pressure spring, a static mixer or a rotor/static mixer. A commercial example of a rotor/static mixer is Ytron-Z homogenizer (shear pump (para 85)”. It would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to include a typical step of in-line adding of ingredients/ enzymes/lactase in a milk processing plant. The ordinary artisan would have been motivated to modify Tossavainen at least for the purpose of streamlining the lactose reducing process and making the process more continuous and energy efficient.
Claims 12 and 15 are rejected under 35 U.S.C. 103 as being unpatentable over Tossavainen and Raj as applied to claim 1 above, further in view of Hendriksen et al., (US 20100285175 A1), hereinafter Hendriksen.
Regarding claims 12 and 15, Tossavainen in view of Raj teach the method of claim 1, however, Tossavainen teaches incubation and skim milk with lactose content overlapping the range as claimed but the prior art does not recite residual enzymatic activity after heat treatment as per claim 12 “wherein after step b), the enzyme retains at least 0.1% of its initial activity, at least 0.5%, at least 1%, at least 2%, at least 10%, at least 50%, at least 80%, at least 90%” and similar recitation of claim 15 is also related to residual enzyme activity of “at least 0.5%, at least 1%, at least 2%, at least 10%” followed by variations of incubation periods of “ 90° C. for 30 seconds, at 140° C. for 5 seconds and at 70° C. for 30 seconds followed by cooling to 0-10° C. and subsequent incubation at 23° C. for 72 hours”.
Although, Tossavainen in view of Raj doe not specify residual activity as instantly claimed (claims 12 and 15), it was known in the art at the time of the effective filing of the invention that properties of enzymes under a given measurement method not only are related to type and source of enzyme but also related to factors like temperature, pH, initial concentration or proportion of enzyme, degree of lactose hydrolysis desired in the finished product. The relationship of above factors to process conditions, e.g., the more the temperature or pH is raised or lowered from the optimal temperature or pH of an enzyme, the lower the residual activity of said enzyme due to the denaturation of said enzyme were known in the art at the time of the effective filing of the invention as taught by Hendricksen in para 231, Table 4 and Table 5 where an example shows a particular lactase enzyme and its activity at various pH values relative to activity of same enzyme at a fixed pH (Table 4) and similarly the activity of same particular lactase enzyme at various temperatures relative to activity of same enzyme at a fixed temperature (Table 5). Thus, the residual or relative enzymatic activity is known to vary based on process conditions in general and as residual enzyme activity % before and after heat treatment in particular.
Given that the method steps of claim 1 taught by Tossavainen in view of Raj is substantially similar and the enzyme taught by applied art is also substantially the same as the claimed enzyme, and it follows that the enzyme activity before and also be substantially similar. As the enzyme of SEQ ID NO:34 in Raj comprises the peptide motif defined in claim 13, it follows that said enzyme(s) should also have the same thermal resistance as in claims 12 and 15. Therefore, in light of the knowledge available to one of ordinary skill in the art at the time of effective filing date of the invention and also in view of teaching provided by Raj and Hendricksen, it would have been obvious to one of ordinary skill in the art that lactase enzyme as taught by Tossavainen and Raj is substantially identical to that of the claims and under similar concentration, when subjected to similar processes will be expected to show residual activity similar to the instantly claimed enzymatic product. The ordinary artisan would have been motivated to modify incubation conditions as taught by Tossavainen and measure enzymatic activity at least to study and determine the storage stability and effectiveness of lactase enzyme itself or storage stability when added to milk based products over various time and temperature conditions at least to determine which enzyme having lactase activity is most cost effective and economical for the particular milk product being made.
Regarding the incubation periods of claim 15, i.e., “after incubation in skimmed milk having a lactose content of 4.7% at 90° C. for 30 seconds, at 140° C. for 5 seconds and at 70° C. for 30 seconds followed by cooling to 0-10° C. and subsequent incubation at 23° C. for 72 hours” see rejection under 35 USC 112 (second paragraph).
It is once again noted that applicant has described the product with parameters and equations which cannot be measured by the office for prior art comparison, because the office is not equipped to manufacture prior art products and compare them for patentability purposes. Therefore, as a prima facia case of obviousness has been properly established, the burden is shifted to the applicant to show that the prior art product is different.
Also see rejection under 35 USC 112 (second paragraph).
Conclusion
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/JYOTI CHAWLA/Primary Examiner, Art Unit 1791
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