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
Claims 1, 11-18, and 21-24 are pending. Claims 16-18 and 21-24 are withdrawn.
Response to Amendment
Applicant amended claim 1 to delete (DP1) and add new limitation “wherein step (i) is performed under conditions that minimize production of maltose as a donor substrate for the transglucosidase”.
The objection to claim 1 is withdrawn in view of the amendment.
Maintained Rejections
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 and 11-15 remain 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 step (i) is performed under conditions that minimize production of maltose as a donor substrate for the transglucosidase”. The claim is indefinite because the metes and bounds of the claim are not clear. It is not clear what conditions the claim requires. It is not clear if the limitations recited in step (i), contacting maltodextrins with an α-amylase to produce malto-oligosaccharides, are the only conditions that the claim requires to minimize production of maltose as a donor substrate for the transglucosidase, or if other conditions such as pressure, temperature, pH, aeration, etc. are required for minimizing production of maltose as
a donor substrate for the transglucosidase.
Claims 11-15, which depend from claim 1, do not cure the deficiency and are also rejected.
Claim Rejections - 35 USC § 103
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.
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.
Claims 1 and 11-14 remain rejected under 35 U.S.C. 103 as being unpatentable over Niu (Electronic Journal of Biotechnology 26 (2017): 46-51, of record in IDS).
Regarding claims 1 and 14, Niu teaches a method of preparation of isomalto-oligosaccharide from hydrolyzed starch using enzyme cocktails composed of α-amylase, pullulanase, β-amylase, and α-transglucosidase to perform simultaneous saccharification and transglycosylation of the hydrolyzed starch (Title, Abstract, 3.5. Improved processes for IMO production). Niu teaches that starch is liquefied to form maltodextrin using α-amylase for starch liquefaction (page 46 right column last para., page 47 para. 2.3). Niu teaches adding α-amylase (BAA), pullulanase (PulA), BBA (β-amylase), and An-TGase (transglucosidase) to the liquified starch (3.5. Improved processes for IMO production). Niu teaches BAA α-amylase catalyzes the hydrolysis of maltodextrin to form malto-oligosaccharides (page 48 right column last para.). Niu teaches varying the β-amylase (BBA) concentration from 0 DP/g to 0.7 DP/g (i.e., 0 DP/kg to 700 °DP/kg) calculated based on dry substrate starch (para. 2.3 and Table 1). Niu teaches that the IMO preparation is done at pH 5 and temperature of 55oC ( Fig. 2C and 2D). Niu teaches using transglucosidase at a concentration of 500 U/g dried starch at 55oC for up to 30 hours (i.e. 500,000,000U/metric ton dry starch) and teaches that the transglucosidase has 360,000 U/g (para. 2.1, para. 2.3, Table 2). Thus, it is understood that the amount of transglucosidase used is equivalent to 1.3 kg of transglucosidase/metric ton of dried starch (500,000,000U*1g/360000U)
While Niu teaches a different concentration of β-amylase than claimed, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the method taught by Niu by optimizing the concentration of the β-amylase enzyme, as suggested by Niu. One of ordinary skill in the art would be motivated to do so in order to enhance the production of isomalto-oligosaccharide. The claimed DP ranges overlap with the DP ranges disclosed by Niu. Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.
Conditions that minimize production of maltose as a donor substrate for the transglucosidase are understood as performing step (i) using α-amylase (Specification [01], [03], [033]). Since Niu teaches that starch is liquefied to form maltodextrin and teaches BAA α-amylase catalyzes the hydrolysis of maltodextrin to form malto-oligosaccharides (i.e., step (i)), then the conditions that minimize production of maltose as a donor substrate for the transglucosidase are met in the teachings of Niu (page 48 right column last para.).
The limitations “wherein the method produces longer chain IMO and/or reduced amounts of glucose compared to a method for producing IMO from maltodextrins using β-amylase instead of said α-amylase in step (i)” and “wherein, after 24 hours of step (ii) at 55-60 °C and pH 4.2-5.2 in the presence of the pullulanase and 1 kg/metric ton dry solids of the transglucosidase, the resulting IMO comprises a glucose content at least 15% lower than the glucose content produced by an otherwise identical method in which B-amylase is used instead of said a-amylase in step (i)” do not require steps to be performed, and therefore, do not limit the method claimed. Whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited. See MPEP 2111.04.
Regarding claims 11 and 13, Niu teaches using a cocktail of enzymes comprising pullulanase, α-amylase, β-amylase, and α-transglucosidase (i.e., simultaneously) (Abstract).
Regarding claim 12, Niu teaches that following the starch liquefication, β-amylase (BBA) was added, followed by addition of α-transglucosidase (An-TGase) (i.e., performed sequentially) (para. 2.3). Niu teaches the starch liquefication in step (1) is done using α-amylase (BLA) and teaches the α-transglucosidase is added in step (3) after the starch liquefication was performed (para. 2.3 steps (1) and (3)). While Niu also teaches using enzyme cocktails (i.e., enzymes added simultaneously) (Abstract), it would be obvious to one of ordinary skill in the art to add the α-amylase first to ensure complete starch liquefication in the optimal conditions of the enzyme such as temperature and pH and then add α-transglucosidase. Since the transglucosidase acts on the product generated from the previous steps and hydrolysis reactions from α-amylase and β-amylase, the sequential addition of the α-amylase would not impede the activity of the α-transglucosidase. Thus, it would be obvious to add the α-amylase and α-transglucosidase sequentially since any order of mixing ingredients is prima facie obvious as stated in MPEP 2144.04IV C.
Claim 15 remains rejected under 35 U.S.C. 103 as being unpatentable over Niu (Electronic J. Biotech. 2017, Vol. 26, pp. 46-51) as applied to claim 14 above, and further in view of Kochhar (Biotechnology letters 12 (1990): 393-396, of record in Office Correspondence mailed on 04/15/2025).
Regarding claim 15, Niu teaches adding Bacillus amyloliquefaciens α-amylase (BAA) to the liquefied starch (page 47 left column para. 3, para. 3.5) and using thermostable α-amylase from licheniformis (BLA) for starch liquefaction (para 2.3). Niu does not teach the liquefying α -amylase and the α-amylase used in step (i) are the same.
However, Kochhar teaches α-amylase from Bacillus amyloliquefaciens is thermostable and liquefying (title). It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further modify the method taught by Niu by using the same α-amylase from Bacillus amyloliquefaciens for the liquefication and the saccharification in step (i), as suggested by Kochhar. One of ordinary skill in the art would be motivated to do so in order to simplify the process and save on the cost of enzymes.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1 and 11-15 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 6, 11, 13, and 23-24 of U.S. Patent No. 7,638,151 in view of Duan (WO 2010118269-A2, published 10/14/2010, of record in Office Correspondence mailed on 11/06/2024) and Niu.
Regarding instant claim 1, patent claim 1 recites a method for making an isomalto-oligosaccharide grain composition said method comprising: (a) contacting an ungelatinized starch in grain (insoluble starch) with an exogenous maltogenic enzyme and a starch liquefying enzyme to produce maltose; (b) contacting said maltose with a transglucosidic enzyme wherein said steps (a) and (b) occur at a temperature less than or at the gelatinization temperature of said starch; and ( c) obtaining a grain composition having an enzymatically produced isomalto-oligosaccharide, wherein said oligosaccharide is obtained from said grain. Patent claim 6 recites wherein said maltogenic enzyme is a beta amylase. Patent claim 11 recites wherein said starch liquefying enzyme is an alpha amylase. Patent claim 13 recites wherein said transglucosidic enzyme is a transglucosidase.
Patent claims 1, 6, 11 and 13 do not recite contacting maltodextrins with an alpha amylase.
However, Duan teaches a method for producing IMO comprising contacting maltodextrins with an alpha amylase (page 34 Example 14). It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the method recited in patent claims 1, 6, 11 and 13 by adding maltodextrin to the ungelatinized starch as suggested by Duan. One of ordinary skill in the art would be motivated to do so since in order to enhance the IMO production. Since Duan teaches that maltodextrins are useful as starch substrates, considered safe food ingredient for human consumption, and are commercially available (page 22 lines 21-30), there is a reasonable expectation of success.
Patent claims 1, 6, 11 and 13 do not recite wherein step (i) is performed in the presence of between 66 to 132 diastatic power (DPo) units β-amylase per kg dry weight maltodextrins.
However, Niu teaches a method of producing IMO using enzyme cocktails composed of pullulanase, α-amylase, β-amylase, and α-transglucosidase to perform simultaneous saccharification and transglycosylation of the hydrolyzed starch (Title, Abstract), and teaches adding β-amylase at varying the concentration from 0°DP/g to 0.7°DP/g calculated based on dry substrate starch (Table 1). Niu teaches that the IMO preparation is done at pH 5 and temperature of 55oC ( Fig. 2C and 2D). Niu teaches using transglucosidase at a concentration of 500 U/g dried starch at 55oC for up to 30 hours. It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further modify the method recited in patent claims 1, 6, 11 and 13 by optimizing the β-amylase concentration, as suggested by Niu. One of ordinary skill in the art would be motivated to do so in order to increase the production of isomalto-oligosaccharide. While Niu teaches a different concentration of β-amylase than claimed, it would be obvious to one of ordinary skill in the art to optimize the concentration of the enzyme. Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.
Regarding instant claim 11, patent claim 23 recites wherein step (a) further comprises contacting said ungelatinized starch with a debranching enzyme. Patent claim 24 recites wherein said debranching enzyme is a pullulanase enzyme.
Regarding instant claim 12, patent claim 1 recites the two steps (a) and (b) separately. It is thus understood the two steps are performed sequentially.
Regarding instant claim 13, patent claim 2 recites wherein said steps (a) and (b) occur concurrently.
Regarding instant claim 14, patent claims 1, 6, 11 and 13 do not recite wherein the maltodextrins are prepared from a starch-containing substrate using a liquefying α-amylase. However, Duan teaches that starch liquefaction is an enzyme-catalyzed step, where starch suspension is gelatinized by rapid heating and alpha-amylases are then used to degrade the viscous liquefact to maltodextrins. Duan teaches that a second enzyme-catalyzed saccharification step, done by an alpha amylase, is required to break down the maltodextrins (page 1 lines 19-27). ). It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further modify the method recited in patent claims 1, 6, 11 and 13 by preparing maltodextrin from a starch-containing substrate using a liquifying α-amylase, as suggested by Duan. One of ordinary skill in the art would be motivated to do so since Duan teaches a more economical substrate such as liquefied starch can be used for IMO production instead of relatively costly high maltose syrup in conventional processes (page 35 lines 14-16). Since Duan teaches a desire to produce IMO, there is a reasonable expectation of success.
Regarding instant claim 15, Duan teaches that PS4, the parent α-amylase of SAS3, displays both endo- and exo-alpha-amylase activity, and teaches that endo-alpha-amylase activity is particularly useful for decreasing the viscosity of gelatinized starch (i.e. liquefying α-amylase), and exo-alpha-amylase activity is particularly useful for breaking down maltodextrins to smaller saccharides (i.e., saccharifying α-amylase ) (page 2 lines 24-29) (i.e., the liquefying α-amylase and the amylase used in step (i) are the same). It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further modify the method recited in patent claims 1, 6, 11 and 13 by using an α-amylase that is both a liquefying α-amylase and an amylase used in step (i) as suggested by Duan. One of ordinary skill in the art would be motivated to do so in order to use less enzymes while at the same time decreasing the viscosity of gelatinized starch and breaking down maltodextrins to smaller saccharides as suggested by Duan.
Claims 1 and 11-15 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 6, 8 and 10 of U.S. Patent No. 8,715,755 in view of Duan and Niu.
Regarding instant claim 1, patent claim 1 recites a method for making any of a food additive, a flour, or an oral rehydration solution containing an isomalto-oligosaccharide grain composition, said method comprising: (a) contacting a ungelatinized grain containing a starch with a maltogenic enzyme and a starch liquefying enzyme to produce maltose; (b) contacting said maltose with a transglucosidic enzyme, wherein said steps (a) and step (b) occur at a temperature less than or at a starch gelatinization temperature; and ( c) obtaining a grain composition having an enzymatically produced isomalto oligosaccharide, wherein said oligosaccharide is derived from said grain. Patent claim 6 recites wherein said maltogenic enzyme is a beta amylase. Patent claim 8 recites wherein said starch liquefying enzyme is an alpha amylase. Patent claim 10 recites wherein said transglucosidic enzyme is a transglucosidase. Patent claims 1, 6, 8 and 10 do not recite contacting maltodextrins with an alpha amylase.
However, Duan teaches a method for producing IMO comprising contacting maltodextrins with an alpha amylase (page 34 Example 14). It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the method recited in patent claims 1, 6, 8 and 10 by adding maltodextrin to the ungelatinized starch as suggested by Duan. One of ordinary skill in the art would be motivated to do so since in order to enhance the IMO production. Since Duan teaches that maltodextrins are useful as starch substrates, considered safe food ingredient for human consumption, and are commercially available (page 22 lines 21-30), there is a reasonable expectation of success.
Patent claims 1, 6, 8 and 10 do not recite wherein step (i) is performed in the presence of between 66 to 132 diastatic power (DPo) units β-amylase per kg dry weight maltodextrins.
However, Niu teaches a method of producing IMO using enzyme cocktails composed of pullulanase, α-amylase, β-amylase, and α-transglucosidase to perform simultaneous saccharification and transglycosylation of the hydrolyzed starch (Title, Abstract), and teaches adding β-amylase at varying the concentration from 0°DP/g to 0.7°DP/g calculated based on dry substrate starch (Table 1). Niu teaches that the IMO preparation is done at pH 5 and temperature of 55oC ( Fig. 2C and 2D). Niu teaches using transglucosidase at a concentration of 500 U/g dried starch at 55oC for up to 30 hours. It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further modify the method recited in patent claims 1, 6, 8 and 10 by optimizing β-amylase concentration, as suggested by Niu. One of ordinary skill in the art would be motivated to do so in order to increase the production of isomalto-oligosaccharide. While Niu teaches a different concentration of β-amylase than claimed, it would be obvious to one of ordinary skill in the art to optimize the concentration of the enzyme. Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.
Regarding instant claim 11, Niu teaches the enzymes comprise pullulanase (Abstract). One of ordinary skill in the art would be motivated to add pullulanase in order to enhance the production of IMO.
Regarding instant claim 12, patent claim 1 recites the two steps (a) and (b) separately. It is thus understood the two steps are performed sequentially.
Regarding instant claim 13, patent claim 2 recites wherein said steps (a) and (b) occur concurrently.
Regarding instant claim 14, patent claims 1, 6, 8 and 10 do not recite wherein the maltodextrins are prepared from a starch-containing substrate using a liquefying α-amylase. However, Duan teaches that starch liquefaction is an enzyme-catalyzed step, where starch suspension is gelatinized by rapid heating and alpha-amylases are then used to degrade the viscous liquefact to maltodextrins. Duan teaches that a second enzyme-catalyzed saccharification step, done by an alpha amylase, is required to break down the maltodextrins (page 1 lines 19-27). It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further modify the method recited in patent claims 1, 6, 8 and 10 by preparing maltodextrin from a starch-containing substrate using a liquifying α-amylase, as suggested by Duan. One of ordinary skill in the art would be motivated so since Duan teaches a more economical substrate such as liquefied starch can be used for IMO production instead of relatively costly high maltose syrup in conventional processes (page 35 lines 14-16). Since Duan teaches a desire to produce IMO, there is a reasonable expectation of success.
Regarding instant claim 15, Duan teaches that PS4, the parent α-amylase of SAS3, displays both endo- and exo-alpha-amylase activity, and teaches that endo-alpha-amylase activity is particularly useful for decreasing the viscosity of gelatinized starch (i.e. liquefying α-amylase), and exo-alpha-amylase activity is particularly useful for breaking down maltodextrins to smaller saccharides (i.e., saccharifying α-amylase ) (page 2 lines 24-29) (i.e., the liquefying α-amylase and the amylase used in step (i) are the same). It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further modify the method recited in patent claims 1, 6, 8 and 10 by using an α-amylase that is both a liquefying α-amylase and an amylase used in step (i) as suggested by Duan. One of ordinary skill in the art would be motivated to do so in order to use less enzymes while at the same time decreasing the viscosity of gelatinized starch and breaking down maltodextrins to smaller saccharides as suggested by Duan.
Response to Arguments
Applicant's arguments filed 08/05/2026 have been fully considered but they are not persuasive.
Applicant argues that claim 1 requires that step (i) be performed using an α-amylase in the presence of a specifically limited amount of β-amylase and, critically, under conditions that minimize production of maltose as a donor substrate for the transglucosidase. Applicant argues that Niu depends on β-amylase to generate maltose as the primary donor molecule driving transglucosylation.
In response to the argument, Niu teaches a novel process for high-efficiency production of IMO comprising contacting a starch slurry with a liquefying α-amylase (BLA) to form maltodextrin and adding to the liquefied starch a mix of α-amylase (BAA), pullulanase (PulA), β-amylase (BBA), and transglucosidase (An-TGase) (2.3 Production of IMOs, 3.5. Improved processes for IMO production, 4. Conclusion, para. 3.1. Effects of the degree of starch liquefaction on IMO yield and page 46 right column last line). Niu teaches that α-amylase (BAA) catalyzes the hydrolysis of maltodextrin to form malto-oligosaccharides (MOSs) and that the addition of a certain amount of β-amylase (BBA) could significantly increase IMO production (3.4. Roles of PulA, BBA, and BAA in IMO preparation). Applicant discloses that contacting starch slurry with α-amylase forms maltodextrins while liquefying with β-amylase produces maltose ([033], [055]). Niu teaches forming maltodextrin and malto-oligosaccharides by α-amylase. Thus, it is understood that Niu’s teaches α-amylase-driven substrate generation to form malto-oligosaccharide from starch.
Applicant argues that the claimed range represents a functional transition point between distinct enzymatic regimes, not a routine optimization of a known parameter. Applicant argues that claim 1 ties the >15% reduction in glucose to a specific and fully recited process, including defined enzyme system, reaction time (24 hours), temperature (55-60 °C), pH (4.2-5.2), and enzyme loading conditions, and requires comparison against a corresponding β-amylase-based process and argues that Niu does not recognize or teach glucose reduction under comparable constraints.
In response to the argument, Niu teaches that the method requires α-amylase (BAA) and that the addition of a certain amount of β-amylase (BBA) could significantly increase IMO production (3.4. Roles of PulA, BBA, and BAA in IMO preparation). Niu teaches varying the β-amylase (BBA) concentration from at 0 DP/g to 0.7 DP/g (i.e., 0 DP/kg to 700 °DP/kg) calculated based on dry substrate starch (para. 2.3 and Table 1). Thus, Niu teaches the limitations of the claim and teaches a range of β-amylase from 0 DP/kg to 700 °DP/kg. One of ordinary skill in the art would be motivated to optimize the concentration of β-amylase in order to optimize the IMO production. The reduction in glucose is understood as the result of the claimed steps. Applicant discloses in Table 11 reaction without α-amylase (OPTIMALT 4G) and with 1188 DPo/kg of β-amylase (reaction 1) has the highest DP1 levels of 32% compared to reactions with α-amylase and β-amylase concentrations varying from 0, 13.2, 26.4, 66, 132, 264, to 660 DPo/kg (reactions 2 to 8 ,respectively) where the DP1 percentage is 21%, 20.9%, 20.9%, 22.0%, 24.6%, 26.9%, and 30.6%, respectively (i.e., DP1 content at least 15% lower than the glucose content produced by reaction without α-amylase but with β-amylase). Applicant discloses the reaction with OPTIMALT®4G (i.e., α-amylase) produces a syrup having much lower DP1 than the traditional reaction with OPTIMALT® BBA (i.e., β-amylase) and discloses that a small amount of β-amylase can be present during the reaction with OPTIMALT® 4G (i.e., α-amylase) without influencing the results significantly, specifically, when there is up to 0.05 kg/MT (i.e., 500 DPo/kg) OPTIMALT® BBA (i.e., β-amylase) present, the DP1 is as low as when no BBA is present (Specification Table 11, [082]).
Applicant argues that the cited patents are directed broadly to enzymatic methods for producing isomalto-oligosaccharides from starch substrates using combinations of maltogenic enzymes, starch liquefying enzymes, and transglucosidase under conditions at or below starch gelatinization temperature and that these processes consistently operate according to a conventional paradigm in which β-amylase is used to generate maltose as the primary donor substrate, whereas instant claim 1 is directed to a materially different process. Applicant argues the cited patents do not disclose or suggest the claimed requirement that the resulting IMO comprises a glucose content at least 15% lower than that produced by a corresponding β-amylase-based method under otherwise identical conditions
In response to the argument, the patent claims are directed to a method for making isomalto-oligosaccharide grain composition and are obvious in view of Duan and Niu. As explained above, Niu teaches contacting maltodextrin with α-amylase to produce malto-oligosaccharides and teaches the presence of β-amylase, pullulanase, and transglucosidase. A glucose content at least 15% lower than that produced by a corresponding β-amylase-based method is understood as the result of contacting maltodextrins with an α-amylase to produce malto-oligosaccharides as disclosed by applicant (Specification Table 11, [082]).
Conclusion
THIS ACTION IS MADE FINAL. 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 nonprovisional extension fee (37 CFR 1.17(a)) 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 mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARY A CRUM whose telephone number is (571)272-1661. The examiner can normally be reached M-F 8:00-5:00 CT with alternate Fridays off.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, LOUISE W HUMPHREY can be reached at 571-272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/MARY A CRUM/ Examiner, Art Unit 1657
/THANE UNDERDAHL/ Primary Examiner, Art Unit 1699
Prosecution Insights