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
Status of the application
2. Claims 21-33 are pending in this office action.
Claims 21-33 have been rejected.
Use Claims
Claim Rejections - 35 USC § 112
3. The following is a quotation of the second paragraph of 35 U.S.C. 112 (b):
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.
4. Claim 23 is rejected under 35 U.S.C. 112, second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
Claim 23 provides for the use of an enzyme which acts on polysaccharides and oligosaccharides having alpha -1,4 glucoside bonds. But since the claim does not set forth any steps involved in the method/process; it is unclear what method/process applicant is intending to encompass. A claim is indefinite where it merely recites a use without any active, positive steps delimiting how this use is actually practiced.
35 USC § 101
5. 35 U.S.C. 101 reads as follows: Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
6. Claim 23 is rejected under 35 U.S.C. 101 because the claimed recitation of a use, without setting forth any steps involved in the process, results in an improper definition of a process, i.e., results in a claim which is not a proper process claim under 35 U.S.C. 101. See for example Ex parte Dunki, 153 USPQ 678 (Bd. App.1967) and Clinical Products, Ltd. v. Brenner, 255 F. Supp. 131, 149 USPQ 475 (D.D.C. 1966).
Claim Rejections - 35 USC § 112
7. 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.
8. Claims 21- 30 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.
9. (a) Independent claim 21 and claim 29 (1) recite “preparing an enzyme which acts on polysaccharides and oligosaccharides having alpha 1, 4 glucoside bonds”. Applicant’s specification recites “The present enzyme is a maltotriosyl transferase, and acts on polysaccharides and oligosaccharides having α-1,4 glucoside bonds as a binding mode to transfer maltotriose units to saccharides (at least in PGPUB in [0054]). Therefore, this “maltotriose unit to saccharides” in line 3 and “by reacting saccharides with maltotriosyl transferase” (in line 4 ) of claim 21 and claim 29 (1) is considered that the terms “saccharides” in lines 3 and 4 as mentioned above, it is the substrate polysaccharides and oligosaccharides for the enzyme maltotriosyl transferase which produces an indigestible saccharide. There is insufficient antecedent basis for this limitation in the claim. Ideally the term “saccharides” should be (at least) “maltotriose units to the poly- and oligo- saccharides” instead of “maltotriose unit to saccharides” only which is converted to produce an indigestible saccharide with the transfer of maltotriose by units by maltotriosyl transferase as claimed in claims 21 and claim 29 (1).
(b) Regarding claim 26 , the phrase "or the like" “beer-like beverage”
renders the claim(s) indefinite because the claim(s) include(s) elements not actually disclosed (those encompassed by "or the like"), thereby rendering the scope of the claim(s) unascertainable See MPEP § 2173.05(d).
Claim Rejections - 35 USC § 103
10. — 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:
(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.
11. The factual inquiries 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 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.
12. Claims 21-23, 25, 27-33 are rejected under pre-AlA 35 U.S.C. 103(a) as being unpatentable over Borchert et al. (WO 2008/092919 A1; cited on the attached Form PTO-892; hereafter “Borchert’”) in view of NPL Lucas et al. ( Lucas et al. June 2009 ; UniPort Accession Number SEQ C5D6S5, November 2010; This is “UniPort C5D6S5’) in view of Duan et al. (US 2005/0031734) and as evidenced by NPL SEQ Alignment (18/829521 SEQ ID #3 vs C5D6S5 of NPL Lucas et al.).
13. It is to be noted that the amendment of claim 1 with the close ended transitional phrase “consists of the amino acid sequence ID #3 does not change the scope of the claim because the office action addressed only one claimed SEQ ID #3 with the disclosed sequence from the prior art by NPL Lucas et al. (Uni-Port C5D6S5). Therefore, the rejection is maintained using identical primary prior art with identical combinations of prior arts of record.
14. Regarding claims 21-23, 29, 31, Borchert discloses that alpha-amylases constitute a group of enzymes that catalyze hydrolysis of starch and other linear and branched 1,4-glucosidic oligo- and polysaccharides (at least in page 3, lines 11-13, 30; ). It is to be noted that Borchert broadly discloses that alpha-amylase can be used in the food processing industry including baking the alpha-amylase into a dough (paragraph bridging pp. 2-3).
Borchert discloses the genetic engineering method of cloning of varieties sources of enzymes including different types of alpha amylase enzymes also (e.g. pages 11, last paragraph, page 12, first paragraph; e.g. alpha amylase gene in Bacillus subtilis to prepare the enzyme alpha-amylase and page 15, under “Nucleic acid construct). Therefore, Borchert et al. discloses (i) a genetic engineering method of preparation of a polypeptide including enzyme from a sequence of interest which is used to make alpha amylase enzyme and (ii) therefore, it also meets alpha amylase enzyme as one additional enzyme in addition to maltotriosyl transferase as claimed in claim 24.
However, Borchert et al. is silent about the sequence of maltotriosyl transferase to make the enzyme from the disclosed genetic sequence.
NPL Lucas et al. teaches a 767 amino acid polypeptide isolated from Geobacillus sp. WCH 70 having alpha amylase activity (page 1, 5-9th lines from top).
NPL Lucas et al. contains 767 amino acid polypeptide isolated from Geobacillus sp. WCH 70 that has greater than 99% amino acid sequence identity to SEQ ID no 3 of the presently claimed invention as also evidenced by NPL SEQ Alignment and also applicants’ own specification (at least in [0030], [0072], See sequence alignment vs Db is C5D656 which is NPL Lucas et al. having disclosed amino acid containing peptide or any peptide having less 34 N-terminal amino acid of NPL Lucas et al. which is identical to claimed SEQ ID#3).
However, NPL Lucas et al. does recite the first 34 amino acid from Geobacillus sp. is not present in SEQ ID#3 (Geobacillus sp. APC9669) which is signal peptide as evidenced by applicants’ own specification (in [0072] of PGPUB and SEQ ID #2 and SEQ ID#2 is identical to NPL Lucas et al. having 767 amino acid containing peptide). Therefore, SEQ ID # 3 from Geobacillus sp. APC9669 is unique as claimed by the applicants which has been deposited on June 2, 2009 as evidenced by applicant’s specification ([O062]- [0066]) and having maltotriosyl transferase activity is reported by the applicant’s claimed invention.
It is also to be noted that applicants have own disclosure that SEQ ID # 2 derived from cloning base sequence (SEQ ID #1) of the gene obtained by original cloning of Geobacillus sp. APC9669. Therefore, NPL Lucas et al. which is identical to SEQ ID #2 (767 amino acid) and identical to claimed SEQ ID #3 (less 34 amino acids at the N- terminal site compared to NPL Lucas et al.).
In this instance, therefore, the claim is broadly and reasonably interpreted as encompassing the maltotriosyl transferase of NPL Lucas et al. recombinantly expressed and isolated using Geobacillus sp. APC9669 as an expression host.
Therefore, the claimed “enzyme product” is broadly and reasonably interpreted as being the maltotriosyl transferase of NPL Lucas et al.
However, it is to be noted that although NPL Lucas et al. with 767 amino acid containing peptide or any peptide having less 34 N-terminal amino acid of NPL Lucas et al. The rest (35 to 767 = 732 amino acid) are identical to claimed SEQ ID#3 (greater than 99% homology as discussed above). It is evidenced from applicant’s specification that this SEQ 767 amino acid (aa) is identical to SEQ Id #2 of Geobacilus spp of applicant’s seq #2 and less 34 aa seq (Signal peptide) is 732 aa which is identical to applicatnt’s SEQ ID #3 and functionality is restored under both the situations because 34 aa represents signal peptide (in PFGPUB [0075]). Therefore, NPL Lucas et al. meets the identical SEQ 100% matching sequence with SEQ ID #3 . NPL Lucas et al. is proper to combine with Borchert et al. to make peptide having maltotriosyl transferase activity from the disclosed identical sequence of NPL Lucas which represents functionally matched (100%) peptide having maltotriosyl transferase using the genetic engineering tool of Borchert et al. to meet claimed invention.
In addition, it is also to be noted that , according to MPEP 2112.01, "Where the claimed and prior art products are identical or substantially identical in structure or composition, a prima facie case of obviousness has been established’. Since the Office does not have the facilities for examining and comparing the claimed protein with the protein of the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed protein and the protein of the prior art (i.e., that the protein of the prior art does not possess the same material structural and functional characteristics of the claimed protein). See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and in re Fitzgeraldet al, 205 USPQ 594.
Therefore, Borchert discloses a method of producing polypeptides having alpha amylase activity by using a nucleic acid construct, expression vector and recombinant host cell comprising the polynucleotides (page 2 under “Summary”, lines 1-25).
As discussed above, NPL Lucas et al. has this identical sequence identity and it encodes maltotriosyl transferase sequence.
Therefore, one of ordinary skill in the art would have been motivated to modify Borchert’s construct by incorporating the polynucleotide sequence of NPL Lucas et al. in order to have the expression of 767 amino acid polypeptide isolated from Geobacillus sp. WCH 70 having alpha amylase activity (page 1, 5-9th lines from top) in order to have desired specific need for its maltotriosyl activity to convert maltotriose (Tri saccharide) to indigestible saccharide as claimed in claims 21, 29, 30, 31, 32 and 33.
It is within the skill of one of ordinary skill in the art to use the genetic engineering method to apply for any available genetic sequence in order to have respective desired product using maltotriosyl transferase as claimed in claims 21, 31, in order to have desired specific need for its maltotriosyl activity to convert maltotriose (Tri saccharide) to indigestible saccharide as claimed in claims 21, 24, 29, 30, 31, 32 and 33. It would have been obvious that indigestible saccharide includes dextrin also as claimed in claims 32, 33. However, claims 24, 32, 33 are also rejected using another secondary prior art by addressing specific claim limitation of alpha amylase (having transglycosylation activity) as claimed in claim 24 and dextrin as indigestible oligosaccharide as claimed in claims 32, 33 and presented below.
It is to be noted that Borchert is analogous prior art. The reason is Borchert et
al. teaches alpha- amylases catalyze hydrolysis of starch and other linear and branched 1 ,4-glucosidic oligo- and polysaccharides and are used in the food processing industry.
One of ordinary skill in the art would have been motivated to express maltotriosyl transferase using NPL Lucas et al. sequence having 99% seq. identical with claimed sequence by modifying Borchert et al.’s expression gene with the reasonable expectation of success to make the polypeptide of NPL Lucas et al. (99% seq. identical as discussed above) (UniPort C5D6S5) having property to make insoluble saccharides from a food comprising starch and other linear and branched 1,4-glucosidic oligo- and polysaccharides as desired need.
Also claim 21 is broad and having any maltotriosyl enzyme. However, 100% matching SEQ ID #3 as discussed above is applicable for the identical properties as claimed in claims 25, 29, 31, 32 and 33.
It is to be noted that the claim limitations of “transfer maltotriose units to saccharides; producing an indigestible saccharide by reacting saccharides with maltotriosyl transferase;” as claimed in claim 21, and claim limitation of claim 22 and “wherein the reaction temperature during the step is from 30°C to 70°C as claimed in claim 25, and the enzymatic properties as claimed in claim 29 and claim 31, these are the claim limitations which claims the substrates and properties of the maltotriosyl transferase enzyme on which the enzyme maltotriosyl transferase acts on to make indigestible saccharide product. As the combinations of prior arts disclose the identical maltotriosyl transferase which meet the identical claimed maltotriosyl transferase having identical structure and therefore, will have identical property e.g. in this instance will act on the identical substrates because of identical substrate specificity property.
Boarchert in view of NPL Lucas et al. is specifically silent about this claim limitation of maintaining the contact with polysaccharide (substrate) and maltotriosyl transferase (Enzyme) in order to perform the substrate enzyme reaction as claimed in claims 21.
However, it would have been obvious that this is known that substrate binds with the enzyme to make the product. It is also to be noted that the claim limitation of “maintaining the contact with polysaccharide (substrate) and maltotriosyl transferase (Enzyme) in order to perform the substrate enzyme reaction as claimed in claim 21”,29 and 31, it is to be noted that when the disclosed sequence is identical to the claimed sequence and makes identical final protein product, the protein product would have identical property e.g. identical claimed maltotriosyl enzyme to perform claimed method step of claim 1 e.g. to be in contact with the substrate produced from the disclosed polynucleotide of NPL Lucas et al. by using the method of Borchert et al. as disclosed by Borchert in view of NPL Lucas et al.
However, (additionally) Duan et al. teaches that isomalto-oligosaccharide (indigestible polysaccharide) is produced by contacting ungelatinized grain containing a starch (i.e. polysaccharide) with a maltogenic enzyme (at least in claim 1 of Duan et al.). It is to be noted that Duan et al. discloses that maltose syrup is contacted with a transglucosidase enzyme to make iso-malto-oligosaccharide ([0084], [0013], at least in claim 1 of Duan et al). Therefore, it reads on maintaining the contact with polysaccharide (substrate) and maltotriosyl transferase (Enzyme) in order to perform the substrate enzyme reaction as claimed in claims 21, 31.
One of ordinary skill in the art would have been motivated to modify Borchert’s in view of NPL Lucas et al. to include the teaching of Duan et al. to allow substrate and enzyme to maintain contact for a desired time and optimum reaction condition in order to have desired product.
Regarding the claim limitation of the reaction temperature above 30-degree C, it is to be noted that as because the disclosed sequence for the enzyme maltotriosyl transferase is identical to the claimed sequence and, therefore, identical to the claimed maltotriosyl transferase enzyme, therefore, it would have the identical property including the reaction temperature above 30-degree C, as claimed in the amended claims 25,31 and discussed in detail below.
It is also evidenced by applicant’s own specification (at least in Fig 1) that the enzyme exhibits stable activity above 30 degree C (e.g. at least in [0017] at about 50 degree C) . Therefore, the identical published prior art sequence (NPL Lucas et al. and see NPL SEQ Alignment) which is identical to claimed SEQ ID#3 and, therefore, will have the identical enzymatic property including Maltotriosyl transferase activity.
15. Regarding claims 27, 28, it is to be noted that the polypeptide of NPL Lucas et al. (Uni-Prot CSD6S5) is encompassed by the claim when the polypeptide of NPL Lucas et al. (Uni-Prot CSD6S5) is considered to be recombinantly produced by Geobacillus sp. APC9669.
16. Regarding claim 29, claim 29 depends on claim 21. Therefore, the rejection made for claim 21 is applicable for claim 29 also. In addition, it is to be noted that an average molecular weight of an amino acid is 110 Da, the disclosed polypeptide of NPL Lucas et al. who teaches 767 amino acids containing polypeptide will have approximately about mol. wt. 84 kDa which encompasses about 83,000 as claimed in claim 13.
It is also understood based on the discussion above that the matching sequence is derived from Geobacillus sp. CSD6S5 and, therefore, the mol. wt. will match in combination with another characteristics property of this enzyme as claimed in claim 29.
It is also evidenced by applicants’ own specification that the enzyme exhibits the identical properties (e.g. at least in claims) and optimum activity at activity at ....and it is the inherent property of the enzyme product made from the identical published sequence (NPL Lucas et al.).
At the time of the invention, it would have been obvious to one of ordinary skill in the art to combine the references of Borchert and NPL Lucas et al. (Uni-Prot C5D6S5) to use the polypeptide of Uni-Prot CS5D6S5 to process a food comprising starch and other linear and branched 1 ,4-glucosidic oligo- and polysaccharides.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to do this because Borchert et al. teaches alpha- amylases catalyze hydrolysis of starch and other linear and branched 1 ,4-glucosidic oligo- and polysaccharides and are used in the food processing industry. One would have had a reasonable expectation of success to use the polypeptide of NPL Lucas et al. (UniProt C5D6S5) to process a food comprising starch and other linear and branched 1,4-glucosidic oligo- and polysaccharides because of the teachings of Borchert and NPL Lucas et al. (UniProt C5D6S5). Therefore, the use of claim 13 would have been obvious to one of ordinary skill in the art at the time of the invention.
However, it is also to be noted that although NPL Lucas et al. with 767 amino acid containing peptide or any peptide having less 34 N-terminal amino acid of NPL Lucas et al. which is claimed SEQ ID#3 (greater than 99% homology as discussed above) does not specifically teach the polypeptide exhibits the functional characteristics and methods as recited in claim 13 according to MPEP 2112.01, "Where the claimed and prior art products are identical or substantially identical in structure or composition, a prima facie case of obviousness has been established’. Since the Office does not have the facilities for examining and comparing the claimed protein with the protein of the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed protein and the protein of the prior art (i.e., that the protein of the
prior art does not possess the same material structural and functional characteristics of the claimed protein). See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgeraldet al, 205 USPQ 594.
17. Claims 30, 32-33 are considered as product by process claim.
The Examiner notes that claims 30-33 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.
17. Claims 24, 32, 33 is rejected under pre-AlA 35 U.S.C. 103(a) as being unpatentable over Borchert et al. (WO 2008/092919 A1; cited on the attached Form PTO-892; hereafter “Borchert’”) in view of NPL Lucas et al. ( Lucas et al. June 2009 ; UniPort Accession Number SEQ C5D6S5, November 2010; This is “UniPort C5D6S5’) in view of Duan et al. (US 2005/0031734) and as evidenced by NPL SEQ Alignment as applied to claim 21 and 31 and further in view of NPL Nakajima et al. (Biosci. Biotechnol. Biochem. 68(11): 2369-2373, 2004).
18. Regarding claims 24, 32, 33, it is to be noted that independent claim 21 is broad and it has ‘comprising’ open ended transitional phrase which can include additional enzyme(s) as claimed in dependent claim 24. Borchert discloses different types of alpha-amylases including the type which constitute a group of enzymes that catalyze hydrolysis of starch and other linear and branched 1,4-glucosidic oligo- and polysaccharides (at least in page 3, lines 11-13, 30; ) e.g. pages 11, last paragraph, page 12, first paragraph; e.g. alpha amylase gene in Bacillus subtilis to prepare the enzyme alpha-amylase). Therefore, claims 24, 32, 33 were rejected with claim 31 also.
However, Borchert et al. is specifically silent about alpha amylase having transglycosylation activity which generates dextrin from malto-oligosaccharide as claimed in claim 24.
NPL Nakajima et al. discloses that a new alpha amylase e.g. Amylase A (page 2369, col 2 first paragraph) having transglycosylation activity produce alpha 1,4 glucan from malto-oligosaccharide as substrate (First paragraph col 1 page 2369). The motivation is to generate alpha 1,4 glucan from malto-oligosaccharide which is cyclic form and is indigestible polysaccharide including dextrin (at least in mid-section of col 1 , page 2369).
It would have been obvious to one of ordinary skill in the art at the time of the invention to include the teaching of NPL Nakajima et al. into Okada et al.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to include alpha amylase to generate alpha 1, 4 glucan from malto-oligosaccharide which is cyclic form and is indigestible polysaccharide including dextrin (at least in mid-section of col 1 , page 2369).
19. Claim 26 is rejected under pre-AlA 35 U.S.C. 103(a) as being unpatentable over Borchert et al. (WO 2008/092919 A1; cited on the attached Form PTO-892; hereafter “Borchert’”) in view of NPL Lucas et al. ( Lucas et al. June 2009 ; UniPort Accession Number SEQ C5D6S5, November 2010; This is “UniPort C5D6S5’) in view of Duan et al. (US 2005/0031734) as applied to claim 1 and further in view of Verbanac et al. USPN 4052226.
20. Regarding claim 26, claim 26 depend on claim 21.
Borchert et al. (genetic engineering method) modified by the genetic sequence of Lucas et al. can make the maltotriosyl transferase enzyme because genetic sequence of NPL Lucas et al. is identical to claimed maltotriosyl transferase as evidenced by applicant’s specification (In specification, SEQ ID#3 which is also claimed in claim 31).
Therefore, it is to be noted that the second part which is the production of “indigestible saccharide” from polysaccharides or oligosaccharide having alpha 1, 4 glucoside bonds can be the substrate for the disclosed maltotriosyl transferase of NPL Lucas et al. which is broadly and reasonably interpreted as being the identical claimed maltotriosyl transferase enzyme property.
However, Borchert et al. in view of Lucas et al. are silent about the first part, “wherein the polysaccharide or oligosaccharide having alpha 1,4 glucoside bond is formed by saccharification of a saccharide ingredient used for producing beer or beer-like beverage” as claimed in claim 26.
Verbanac et al. discloses that saccharification of wheat, barley, corn starch etc. containing saccharide ingredients having alpha 1, 4 glucosidic bond ( col 3 lines 56-62 and col 4 lines 30-40) col 3 lines 56-62) and therefore, can be the substrate for maltotriosyl-transferase enzyme.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Borchert et al. in view of Lucas et al. to include the teaching of Verbanac et al. to make perform saccharification of commonly available starch source from wheat, barley, corn starch etc.in order to make saccharified saccharide having alpha 1, 4 glucosidic bond which is ready to be available to react with maltotriosyl transferase in order to make indigestible saccharide.
Conclusion
21. One pertinent prior art by Tanaka (USPN 5698245 from 14/024277) notes that addition of maltotriose-forming enzyme to wheat flour cleaves the alpha-1,4-bonding in the wheat flour (column 6, lines 18-27). Tanaka teaches an example of the maltotriose-forming enzyme is maltotriose-forming enzyme from Streptomyces griseus (p. 3, lines 19-20)
22. 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
Prosecution Insights