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. Applicants’ arguments and amendments filed on 6/26/2026 overcomes the rejections of record. However, the new grounds of rejection as set forth below are necessitated by applicants’ amendment and therefore, the following action is Final.
Any objections and/or rejections made in the previous action, and not repeated below, are hereby withdrawn.
Status of the application
3. Claims 1-5, 7-11, 14- 17 are pending in this office action.
Claims 1-5, 7-11, 14- 17 have been rejected.
Claim Rejections - 35 USC § 103
4. 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.
5. 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.
6. The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
7. Claim(s) 1, 5, 14, is/are rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (US 2014/0227393 A1) in view of Cramer et al. (WO 2020/117548 A).
8. It is to be noted that independent claim 1 claims (i) two enzymes “ordinary lactase” and beta galactosidase with transgalactosylation activity are used to make lactose-free dairy product prior to fermentation (ii) No heat treatment of beta galactosidase with transgalactosylation activity.
9. Regarding claim 1, Chen et al. discloses (iii) beta galactosidase with transgalactosylation enzyme activity which hydrolyzes lactose and generates GOS ([0019]) having 0.8 to 1.2% (w/w) lactose and GOS ([0019], [0033]) followed by fermentation ([0034]) to make fermented product. Chen does not teach the heat inactivation of the enzyme beta galactosidase with transgalactosylation activity in between, i.e. prior to fermentation and after the enzyme treatment step ([0033], [0034]).. Therefore, it meets the claim limitation of “heat inactivation of this beta galactosidase enzyme is omitted” which meets the claim limitation of amended independent claim 1.
Chen et al. discloses residual lactose about 0.8-1.2% (w/w) is present in the enzyme hydrolyzed milk material ([0033]) to conduct lactic fermentation reaction ([0034]) as discussed above. Claim 1 claims “fermenting Lactose-free”. It is evidenced from applicants specification that <0.2% lactose or <0.1 % or 0% lactose is considered lactose-free (in PGPUB [0050]).
Therefore, Chen et al. is silent about making lactose-free hydrolyzed milk to be treated with the added “ordinary lactose” in combination with beta galactosidase with transgalactosylating enzyme to make the hyrolyzed product having minimal/nil lactose and is ready to be fermented in the next step.
Cramer et al. discloses the treatment to hydrolyze lactose using beta galactosidase with transgalactosylating enzyme (at least in claims 1, 2, 4) and "a lactase" is the lactase from K. lactis (at least in claim 1,17 of Cramer et al.) which is claimed "ordinary lactase" and the combined treatment makes GOS with minimal lactose (0.01% lactose) present in the hydrolyzed product (in claims 1, 17, 42, 43 of Cramer et al.). Cramer et al. discloses that remaining lactose is treated with lactase enzyme which is without transgalactosylating activity (at least in claim 1, 17 of Cramer et al.) and is used to further degrade residual lactose present after completion of the treatment with a transgalactosylating enzyme (in claim 1, 17 of Cramer et al.) in order to have 0.01% lactose i.e. minimal/no lactose (is below 0.01% lactose) after completion of the treatments with a transgalactosylating enzyme followed by (another) "lactase" (without transgalactosylating activity) to degrade the remaining lactase (in claims 1, 17, 42, 43 of Cramer et al.). Therefore, Chen in view of Cramer et al. teach "lactose-free” dairy product as claimed in independent method claim . It is evidenced by applicant’s specification that 0.01% lactose is considered as “lactose -free” (at least in PGPUB [ 0050]).
As discussed above, Cramer et al. discloses that remaining lactose is treated with lactase enzyme which is without transgalactosylating activity (at least in claim 1, 17 of Cramer et al.) and is used to further degrade residual lactose present after completion of the treatment with a transgalactosylating enzyme (in claim 1, 17 of Cramer et al.) which meets claim 5.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Chen et al. with the teaching of Cramer et al. to use lactase enzyme after completion of the treatments with a transgalactosylating enzyme in order to degraded residual lactase further by another " lactase" enzyme (in claim 1 of Cramer et al.) to make “lactose-free” dairy product ready to be fermented (i.e. prior to fermentation) further in order to make fermented lactose-free dairy product as per desired choice for desired use.
Regarding the claim limitation " wherein the ß-galactosidase with transgalactosylation activity decomposes lactose in the dairy product starting material to galactose and glucose, and transfers galactose obtained through decomposition onto a hydroxyl group of lactose in the dairy product starting material to achieve conversion to galactooligosaccharides, and optionally, the ß-galactosidase with transgalactosylation activity transfers galactose obtained through decomposition onto a hydroxyl group of the galactooligosaccharides to achieve conversion to higher-order galactooligosaccharides" as claimed in claim 1, it is the inherent property of transgalactosylating enzyme and therefore, it achieves GOS production.
Cramer et al. also discloses the property of beta galactosidase with transgalactosylation activity. This is known property of this enzyme. Therefore, even if it is under background section, page 1 of Cramer et al., it is considered in this respect. Cramer mentioned that the property of "The enzyme b-galactosidase (EC 3.2.1.23) usually hydrolyses lactose to the monosaccharides D-glucose and D-galactose. In the normal enzyme reaction of b- galactosidases, the enzyme hydrolyses lactose and transiently binds the galactose monosaccharide in a galactose-enzyme complex that transfers galactose to the hydroxyl group of water, resulting in the liberation of D- galactose and D-glucose. However, at high lactose concentrations some b- galactosidases are able to transfer galactose to the hydroxyl groups of D- galactose or D-glucose in a process called transgalactosylation whereby galacto-oligosaccharides are produced. At high lactose concentrations some b -galactosidases are able to transfer galactose to the hydroxyl groups of lactose or higher order oligosaccharides (in Background section, second paragraph). Therefore, based on the above discussion, Cramer et al. anticipates the claimed property of " wherein the ß-galactosidase with transgalactosylation activity decomposes lactose in the dairy product starting material to galactose and glucose, and transfers galactose obtained through decomposition onto a hydroxyl group of lactose in the dairy product starting material to achieve conversion to galactooligosaccharides, and optionally, the ß-galactosidase with transgalactosylation activity transfers galactose obtained through decomposition onto a hydroxyl group of the galactooligosaccharides to achieve conversion to higher-order galactooligosaccharides" as claimed in claim 1.
Regarding claim 14, The Examiner notes that these are product-by-process claims.
Therefore, it is to be noted that, in this case, the courts have held that when the prior art factor appears to differ from the claimed factor only in the method of obtaining the factor, the burden of persuasion was on applicant to show that the claimed product exhibited unexpected properties compared with that of the prior art. The courts further noted that “no objective evidence has been provided establishing that no method was known to those skilled in this field whereby the claimed material might have been synthesized.” 10 USPQ2d at 1926.
The courts also held that “even though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process.” In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985) (citations omitted).
Furthermore, "[b]ecause validity is determined based on the requirements of patentability, a patent is invalid if a product made by the process recited in a product-by-process claim is anticipated by or obvious from prior art products, even if those prior art products are made by different processes." Amgen Inc. v. F. Hoffman-La Roche Ltd., 580 F.3d 1340, 1370 n 14, 92 USPQ2d 1289, 1312, n 14 (Fed. Cir. 2009). See MPEP §2113.
Lastly the courts have held that when the prior art discloses a product which reasonably appears to be either identical with or only slightly different than a product claimed in a product-by-process claim, a rejection based alternatively on either section 102 or section 103 of the statute is eminently fair and acceptable. As a practical matter, the Patent Office is not equipped to manufacture products by the myriad of processes put before it and then obtain prior art products and make physical comparisons therewith.” In re Brown, 459 F.2d 531, 535, 173 USPQ 685, 688 (CCPA 1972). The examiner further notes that “The Patent Office bears a lesser burden of proof in making out a case of prima facie obviousness for product-by-process claims because of their peculiar nature” than when a product is claimed in the conventional fashion. In re Fessmann, 489 F.2d 742, 744, 180 USPQ 324, 326 (CCPA 1974). Once the examiner provides a rationale tending to show that the claimed product appears to be the same or similar to that of the prior art, although produced by a different process, the burden shifts to applicant to come forward with evidence establishing an unobvious difference between the claimed product and the prior art product. In re Marosi, 710 F.2d 798, 802, 218 USPQ 289, 292 (Fed. Cir. 1983). See MPEP §2113.
10. Claim(s) 2-4, is/are rejected under 35 U.S.C. 103 as being unpatentable over are rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (US 2014/0227393 A1) in view of Cramer et al. (WO 2020/117548 A) as applied to claim 1 and further in view of Almudena et al. (US 2019/0008176 A1).
11. Regarding claims 2-4, Cramer et al. does not specifically teach the individual amount of "beta galactosidase with transgalactosylation enzyme" and "ordinary lactase enzyme" and their ratio.
It is to be noted that Cramer et al. discloses both the beta galactosidase with transgalactosylation enzyme and "a lactase enzyme" (i.e. claimed "ordinary lactase") to meet claim 1. Cramer et al. also discloses that after the action of beta galactosidase with transgalactosylation enzyme, residual lactose is further hydrolyzed by adding another disclosed "a lactose" as disclosed by Cramer et al. (at least in claim 1 of Cramer et al. ) which reads on ""ordinary lactose" as claimed in independent claim 1.
As it is enzyme substrate reaction, therefore, it is within the skill of one of ordinary skill in the art to optimize the amount of enzyme to be added in order to convert mostly all lactose into minimal/nil lactose to make lactose-free dairy product.
However, more specifically, examiner has considered one secondary prior art by
Almudena et al. who discloses the range amount of lactase enzyme used to hydrolyze lactose from dairy product raw material and discussed below. This disclosure is beneficial because it provides an additional guideline of the range amount of the individual amounts of these enzymes with respect to dairy product starting material, which is beneficial to one of ordinary skill in the art to optimize the amount and ratio by considering the optimization of the enzymes from within the disclosed range amounts as disclosed by Almudena et al.
Almudena et al. discloses that ([0097]) The lactase is advantageously added in an amount of 0.005 wt. % to 0.20 wt. %, in particular 0.01 wt. % to 0.15 wt. %, preferably 0.02 wt. % to 0.06 wt. %, based on the total weight of the dairy product ([0097], [0098]) which amount is applicable to any kind of lactase ([0096], Table 1). It is to be noted that Almudena et al. discloses that lactase can be added any time including before fermentation to the dairy product (0098]). Therefore, the amount of the enzyme lactase can be considered when it is added directly to a dairy product starting material also. As the disclosed amount of enzyme is applicable for any kind of lactase enzyme ([0096]), therefore, it meets claimed amounts of the enzymes as claimed in claims 2,3, 4. It also overlaps the claimed ratio of the enzymes as claimed in claims 2-4. It is to be noted that the claimed 0.5-12.0 g is 0.05% -1.2% by weight of dairy product raw material. Therefore, it shows prima facie case of obviousness according to MPEP 2145.05. In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990).
Absent showing of unexpected results, the specific amount of lactase enzymes is not considered to confer patentability to the claims. As the transgalactosylation enzyme activity with respect to lactase activity within the betagalactosidase enzyme and also the residual lactose present after betagalactosidase with transgalactosylation enzyme action are variables that can be modified, among others, by adjusting the amount of two lactase enzymes 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 chocolate (4) in Cramer et al.in view of Almudena et al., to amounts, including that presently claimed, in order to obtain the desired effect e.g. desired lactose hydrolysis to make lactose-free dairy product. (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).
11. Claims 8-11 and 15, are rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (US 2014/0227393 A1) in view of Cramer et al. (WO 2020/117548 A) as applied to claim 1 and further in view of Arat M et al. (TR 201820107 A2).
12. Regarding claim 8, Chen et al. in view of Cramer et al. disclose milk -based substrate raw material. However, they are specifically silent about concentrated milk. Therefore, additionally claim 8 is rejected here with claims 9-11 in order to address "concentrated milk" of claim 8.
Cramer et al. does not specifically teach "milk has more than 5% lactose" of claim 9, and not less than 5% as claimed in claim 15 and more than 4.0% protein of claim 10 and concentrated milk is concentrated by any type of filtration or/and reverse osmosis method as claimed in claim 11.
Arat et al. discloses that raw milk can be separated into fractions using filtration method ([0053]) where milk protein cannot pass through membrane ([0051]) and retained fraction with high protein is mixed with desired amount of lactose including lactose containing permeate having at least 7% by wt. of lactose ([0055]) in order to have desired sweetness after hydrolysis step of lactose by lactase enzyme ([0014], [0017], [0046]-[0048], [0053], [0054], [0055]).
13. Regarding claim 9, Cramer et al. discloses that the milk-based substrate has lactose content 1-60% (w/w) (First paragraph under "Summary of The Invention" and claim 2 of Cramer et al.). Arat et al. discloses concentrated milk can have at least 7% by wt. of lactose ([0055]). Therefore, the disclosed range amount of lactose overlaps claimed at least 5% by weight of lactose of claim 9. It shows prima facie case of obviousness according to MPEP 2145.05. In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990).
It is evidenced by applicants' own specification that cow's milk contain protein 3.2-3.8% by weight and concentrated form has 5-9% by weight of protein (in PGPUB [0046]). Therefore, the retained fraction using filtration method which is a ‘concentrated milk’ and retains mainly protein has higher amount of protein i.e. including "no less than 4% by weight" of protein as claimed in claim 10.
One of ordinary skill in the art would have been motivated to modify Chen et al. with the teaching of Arat et al. to consider another lactase to be introduced into Chen et al. in order to further hydrolyze the residual lactose into glucose and galactose in order to have desired sweetness of the final product ( at least in ([0014], [0017], [0046]-[0048], [0053], [0054]) and not to have too much undesired sweetness taste ([0055]) because of predominant formation of nutritionally enriched GOS in the final product.
Therefore, Cramer et al. in view of Arat et al. meet claims 8-11.
14. Claim 16 is rejected under 35 U.S.C. 103 as being unpatentable over are rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (US 2014/0227393 A1) in view of Cramer et al. (WO 2020/117548 A) and further in view of Arat M et al. (TR 201820107 A2) as applied to claim 8 and further in view of Hendriksen et al. (US 20180295846 A1).
15. Regarding claim 16, it is to be noted that claim 16 depends on claim 8. Therefore, the rejection made for claim 8 to address “concentrated milk” is applicable for claim 16 also.
However, Chen et al. in view of Cramer et al. and Arat et al. are specifically silent about “concentrated milk comprises added fat” as claimed in claim 16.
Hendriksen et al. discloses broadly many types of milks including condended milk as starting dairy material ([0060]) to be used as substrate for this type lactase treatment to make fermented lactose-free product may be from starting material (at least in [0060]). Hendriksen et al. also discloses that the above dairy product may additionally comprise additional components, e.g. vegetable oil etc. (at least in [0061]) which meets claim 16.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Chen et al. in view of Cramer et al. and Arat et al., to include the teaching of Hendriksen et al. also discloses that [0061] the above dairy product may additionally comprise additional components, e.g. vegetable oil etc. ([0061]) which meets claim 16.
16. Claim 17 is rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (US 2014/0227393 A1) in view of Cramer et al. (WO 2020/117548 A) as applied to claim 1 and further in view of Brunkhurst et al. USPN 2412203.
17. Regarding claim 17, Chen et al. in view of Cramer et al. and Arat et al. are silent about starting material is “concentrated milk combined with cream” as claimed in claim 17.
Brunkhurst et al. discloses a method of making a frozen whole milk product from which a reconstituted whole milk may be made comprising separating fresh whole milk into cream and skim milk, subjecting the cream to a sufficiently high temperature to pasteurize it without removing volatile matter, subjecting the skim milk to pasteurizing temperature to reduce the water content in a concentration ratio by volume of between 21/2 to 1 and 4 to 1, homogenizing the hot concentrated milk and cream together to break up the solids reducing the temperature of the homogenized mixture to normal room on tap water temperature and subjecting the mixture without substantial delay to a sufficiently low temperature to quickly bring the mixture to a temperature of between zero and -40° F. to the frozen whole milk product (At least in claim 1 of Brunkhurst et al.) which product is convenient for storage in bulk amount compared to regular whole milk for a long time under frozen condition and it has its appearance and consistency and taste of regular whole milk when added water for consumption (at least col 1 lines 15-30).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Chen et al. in view of Cramer et al. and Arat et al. to include the teaching of Brunkhurst et al. to treat raw milk to concentrate and to separate cream from milk and then combining them together in order to obtain concentrated milk combined with cream which can be kept frozen (At least in claim 1 of Brunkhurst et al.) and is convenient for storage in bulk amount compared to regular whole milk for a long time under frozen condition and it has its appearance and consistency and taste of regular whole milk when added water for consumption (at least col 1 lines 15-30).
18. Claims 1, 7, rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (US 2014/0227393 A1) in view of Arat et al. (TR 201820107 A2).
19. It is to be noted that independent claim 1 claims (i) two enzymes “ordinary lactase” and beta galactosidase with transgalactosylation activity are used to make lactose-free dairy product prior to fermentation (ii) No heat treatment of beta galactosidase with transgalactosylation activity.
19. Regarding claim 1, Chen et al. discloses beta galactosidase with transgalactosylation enzyme activity which hydrolyzes lactose and generates GOS ([0019]) having 0.8 to 1.2% (w/w) lactose and GOS ([0019], [0033]) followed by fermentation ([0034]) to make fermented product. Chen does not teach the heat inactivation of the enzyme beta galactosidase with transgalactosylation activity in between, i.e. prior to fermentation and after the enzyme treatment step ([0033], [0034]).. Therefore, it meets the claim limitation of “heat inactivation of this beta galactosidase enzyme is omitted” which meets the claim limitation of amended independent claim 1.
However, Chen et al. discloses residual lactose about 0.8-1.2% (w/w) is present in the enzyme hydrolyzed milk material ([0033]) to conduct lactic fermentation reaction ([0034]) as discussed above. Claim 1 claims “fermenting Lactose-free”. It is evidenced from applicants’ specification that <0.2% lactose or <0.1 % or 0% lactose is considered lactose-free (in PGPUB [0050]).
Therefore, Chen et al. is silent about making lactose-free hydrolyzed milk to be made with the added “ordinary lactose” in combination with beta galactosidase with transgalactosylating enzyme to make the hydrolyzed product having minimal/nil lactose and is ready to be fermented in the next step.
Arat et al. discloses that membrane concentrated raw milk with more lactose having at least 7% by wt. of lactose ([0055]) can be treated with lactase enzyme in order to have desired sweetness achieved with the generation of glucose and galactose after hydrolysis step of lactose ([0014], [0017], [0046]-[0048], [0051], [0053], [0054], [0055]) with the removal of lactose.
It would have been obvious that one of ordinary skill in the art would have consider to include lactase (i.e. ordinary lactose) in combination with beta galactosidase with transgalactosylation activity containing lactose to the modify Chen et al. because Chen’s betagalactosidase provides enzyme hydrolyzed milk having 0.8 -1.2% (w/w) lactose (in Chen et al. [0033]), and therefore, needs to be lactose -free product. It would have been obvious that these two enzymes share common function of ‘similar lactose hydrolysis activity’, and, therefore, can be added simultaneously because they are compatible and meet claim 7.
One of ordinary skill in the art would have been motivated to modify Chen et al. with the teaching of Arat et al. to consider another lactase to be introduced into Chen et al. in order to further hydrolyze the residual lactose into glucose and galactose in order to have desired sweetness of the hydrolyzed product ( at least in ([0014], [0017], [0046]-[0048], [0053], [0054]) with the removal of residual lactose.
Response to arguments
20. Applicants’ arguments and amendments overcome rejections of record. The reason is prior used two primary prior arts by Cramer et al. (at least in Example 3) and Silver et al. ([0096]) disclose heat inactivation of beta galactosidase with transgalactosylation activity which is “omitted” in the amended claim 1 of the claimed invention.
Examiner has considered new primary prior art by Chen et al. who discloses beta galactosidase with transgalactosylation enzyme activity which hydrolyzes lactase ([0019]) and no heat treatment is necessary to inactivate this enzyme before fermentation ([0033], [0034]).
However, examiner has considered Cramer et al. as secondary prior art to consider additional combination of lactase with motivation as discussed in detail in this office action. Cramer et al. was not used to reject claim 7 in the last office action.
Examiner has maintained the rejection of claim 7 with prior secondary prior art by Arat et al. who also discloses ‘lactase’ to be added simultaneously in order to maintain the prior rejection proper in order to make final office action.
There is no further arguments.
The rejection is made as final.
Conclusion
21. One pertinent prior art by Lida et al. (USPN 4237230 A) teaches a novel lactase is useful for treating milk and milk products as well as for preventing diarrhea due to lactose intolerance, especially in babies and infants (Abstract and second paragraph under Background section). This can be combined with Chen as secondary prior art. However, Cramer was used before and it has both the ordinary lactase and beta galactosidase . Therefore, Cramer is used. This can also be used to reject claim 7.
22. Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
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
/ERIK KASHNIKOW/Supervisory Patent Examiner, Art Unit 1792
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