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 .
Priority
This application is a 371 of PCT/CA2020/051734 filed 12/16/2020 which claims benefit of provisional application 62/950,354 filed 12/19/2019. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 09/18/2025 complies with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Status of the Claims
Claims 1-3, 5-17 and 25-42 are pending. Claims 26-42 were withdrawn. Claims 1, 2, 5-10 and 12-16 are amended. Claim 4 is cancelled.
Claims 1-3, 5-17 and 25 (claim set filed 08/07/2025) and are examined on the merits herein.
Withdrawal of Rejections
The response and amendment filed on 08/07/2025 are acknowledged. All of the amendment and arguments have been thoroughly reviewed and considered.
For the purposes of clarity of the record, the reasons for the Examiner's withdrawal and/or maintaining if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner's response to arguments section.
Submission of corrected drawings on 08/07/2025 is acknowledged. Drawings are accepted.
The previous objection to specification has been withdrawn necessitated by submission of substitute specification on 08/07/2025.
The previous claims 1, 4, 7, 9, 12, 14 and 15 objections have been withdrawn necessitated by amendment of claims 1, 7, 9, 12 and 14 and cancellation of claim 4.
The previous claims 1-17 and 25 rejections under 35 U.S.C. 112(b) have been withdrawn necessitated by amendment of claims 1, 2, 5-7, 9 and 14 and cancellation of claim 4.
New 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 1-3, 5-17 and 25 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.
Amended claim 1 recites method steps for preparing a resistant IMO-R. Step (a) is directed to preparing a liquified starch from starch slurry. Step (b) is directed to adjusting pH of the starch slurry to about 4.5 to 5.5 by performing steps (i) –(viii) and results in producing liquified starch at final step (viii). It is not clear: (i) how step (b) can be directed to starch slurry if liquified starch was already obtained in step (a) according to claim 1; (ii) how performing steps (i)-(viii) comprising adjusting pH to about 6.3 to 6.7, enzymatic reaction with α-amylase and branching enzymes and adjusting temperature can result in adjusting pH to about 4.5 to 5.5. The specification describes preparation of liquified starch by treatments recited in steps (i)-(viii) prior to adjusting pH to 4.5 to 5.5 (paragraphs 0075, 0076). Thus, it seems that steps (i)-(viii) should be included in step (a) and not (b). The scope and boundaries of claim 1 are not certain making claim 1 indefinite.
Claims 2, 3, 5-17 and 25 dependent on claim 1 do not resolve the issue mentioned above and are rejected.
Additionally, the same uncertainty is present in claims 9 and 15. Claim 9 reads as directed to treatment with GTase prior to adjusting pH of the starch slurry to about 4.5 to 5.5 and hence prior to the steps (i)-(viii) of preparing liquified starch. Similarly, claim 15 recites treatment of starch slurry with GTase and CGTase prior to step (b) of claim 1. It is not clear how GTase treatment can be performed on the starch slurry and not liquified starch since the specification describes that treatments with GTase are performed on liquified starch and not starch slurry after steps (i)-(viii) are performed. Figure 1 presents the schemes of the treatment wherein enzymatic scheme A corresponds to claim 1, scheme C to claim 9 and scheme F to claim 15. As can be seen in all schemes treatments start with BE – branching enzyme treatment recited in claim 1 step (v), one of the steps of producing liquified starch, and GTase treatment are not performed on starch slurry prior to BE step.
For examination claim 1 is interpreted as preparing liquified starch by steps (a) and (i)-(viii) and step (b) directed to adjusting pH to about 4.5 to 5.5 prior to treatment with a second α-amylase in step (c). Claims 9 and 15 are interpreted as directed to adjusting pH of the liquified starch obtained in steps (i)-(viii) of claim 1 to about 6.5 to 8.0 and then treating with GTase (for claim 9) and GTase and CGTase (for claim 15) prior to adjusting pH to about 4.5 to 5.5 and further treatment with a second α-amylase in step (c).
Claim 1 was amended to recite “a first α-amylase enzyme (Kleistase) and a second α-amylase enzyme (Fungamyl 800L). It is not clear if enzyme names in parenthesis are limiting to the claim since they represent specific α-amylases. The scope and boundaries of the claim are not certain making claim indefinite.
Additionally, Kleistase and Fungamyl 800L are trademark/trade names. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, although Kleistase and Fungamyl 800L were identified as α-amylases, the trademark or trade name is still recited making claim indefinite. The same tradename or trademarks/trade names are present in claims 2, 5 and 7.
Claims 2, 3, 5-17 and 25 dependent on claim 1 do not resolve the issue mentioned above and are rejected.
Response to Arguments
Applicant's arguments filed 08/07/2025 have been fully considered but they are not persuasive.
Applicant argues (addressing p. 14-15 of the Remarks) that: “With respect to claims 1, 2, and 4-6 concerning the use of tradenames, the claims have been amended to: replace the term "Kleistase" with "a first α-amylase enzyme (Kleistase)"; replace the term "Fungamyle 800L" with " α second a-amylase enzyme (Fungamyl 800L)"; and replace the term "Branchyme" with "an oligosaccharide branching enzyme (BE)". The use of the tradename is now presented as an acronym for that term or element throughout the remainder of the claims.
These arguments are not persuasive for the reasons discussed in the rejection. Further the amendment does not merely make the term an acronym. The claim causes issues in clarity as discussed above.
Maintained/Modified Rejections
The following rejections are maintained and/or modified taking into consideration amendment to claims filed on 08/07/2025.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-3, 5, 6 and 25 are rejected under 35 U.S.C. 103 as being unpatentable over Chockchaisawasdee (Chockchaisawasdee and Poosarah J. Sci. Food Agric., 2013, 93, 180-186) in view of Thang (Thang et al. Appl. Biochem. Biotechnol., 2010, 161, 157- 170), Khatoon (Khatoon et al. Food Res. Internat., 2009, 42, 1426-1433), Lee (Lee et al. PLOS One, 2013, 8, e59745, 1-10 on record in IDS) and Niu (Niu et al. Electronic J. Biotechn., 2017, 26, 46-51 on record in IDS).
Regarding claim 1, Chockchaisawasdee teaches production of IMO-R from banana flour by liquefaction of banana slurry with Thermamyl SC enzyme which is an α-amylase (p. 181, left column, 2nd paragraph and p. 181, right column, 3rd paragraph). Chockchaisawasdee describes preparation of 500 g banana slurry with the concentration of 250 g/kg which is 25% weight by volume, adjustment of pH of the slurry with NaOH to pH 5.5-6, addition of 0.15 ml of Thermamyl SC, incubation at 93-95°C with agitation till unhydrolyzed starch is not detected and stopping the reaction by boiling for 5 min and cooling after that to ambient temperature. The saccharification is performed with a second α-amylase, Fungamyl 800L (p.181, left column, 2nd paragraph), and IMO-R synthesis with transglucosidase (Abstract). Chockchaisawasdee describes that saccharification of liquefied slurry is performed by Fungamyl 800L at pH 5.5-6 at 50° C with constant agitation for 24h, followed by inactivation at 95° C for 10 min (p. 181, right column, 5th paragraph). Transglucosylation is performed with Transglucosidase L at pH 5.5 (adjusted at ambient temperature) at 60° C for 24h followed by inactivation at 95° C for 5 min (p. 182, left column, 1st paragraph). Thus, Chockchaisawasdee teaches the instant method steps (b) -(j) with similar parameters except for the time of saccharification of 30 min and time for inactivation for 30 min in instant application. Please see claim interpretation regarding step (b) in 112(b) rejection.
Chockchaisawasdee does not teach Kleistase and Branchzyme during preparation of liquified starch, does not teach tapioca starch, does not teach monitoring and reaching the recited DE and does not teach IMO-R to be digestion-resistant to human gut enzymes.
Thang teaches fermentation of cassava starch for production of acetone-ethanol-butanol (Abstract). Thang discloses liquefaction of cassava starch prior to saccharification performed by Kleistase which is an α-amylase from Bacillus subtilis (p. 160, 3rd paragraph). For the reaction 90 g of cassava flour is suspended in water to 400 ml (that makes 22.5%), 0.3% (v/v) of Kleistase is added and reaction is carried out at pH 6.0, at 95°C for 2h (p. 160, 3rd paragraph). Parameters for the reaction with Kleistase in Tang teaching are close to claimed parameters.
Khatoon teaches partial hydrolysis of corn, rice and tapioca starches with heat stable α-amylase (Abstract). Khatoon discloses that hydrolysis of starch samples (10-20% w/v) for 30 min at 90 +/- 2°C resulted in DE of 8-12 (Abstract). Khatoon confirms partial hydrolysis by showing marked decrease in solid properties of starches and presence of oligosaccharides with broad molecular weight distribution (Abstract).
Lee teaches generation of the highly branched maltodextrins that are slowly digestible (Abstract). To prepare highly branched maltodextrins Lee is using branching enzyme, Branchzyme (p. 4, left column, 3rd paragraph). Lee describes treatment of boiled corn starch with 500 U/g of dry weight of starch with Branchzyme at 65°C and pH 6.5 for 24 h (p. 4, right column, 2nd paragraph). After the reaction Branchzyme is inactivated by boiling for 10 min (p. 5, left column, 1st paragraph). Parameters of Branchzyme reaction in Lee teaching cover the corresponding claimed limitations of steps (v) and (vi). Lee teaches hydrolysis of the modified starches by human pancreatic α-amylase followed by hydrolysis with mucosal α-glucosidases (p. 7, left column, last paragraph and right column, 1st paragraph). Lee discloses that hydrolysis showed the slow digesting property of the prepared starches (Abstract).
Niu teaches preparation of isomalto-oligosaccharides (IMO) from starch (Abstract). Niu describes liquefaction of corn starch with α-amylase (p. 47, right column, 3rd paragraph). Niu discloses that during liquefaction of the corn starch samples were collected to determine dextrose equivalent (DE). (p. 47, right column, 3rd paragraph). Niu describes obtaining liquefied starch with DE values of 12, 20 or 30 (p. 48, left column, 2nd paragraph). The liquefied starch was used for saccharification and transglycosylation. Niu discloses that for scale-up preparation of IMOs liquified starch with DE value of approximately 25 was used (p. 47, right column, 3rd paragraph). Niu mentions that increasing DE shortened transglycosylation time and was beneficial to IMO formation with increased yields per reaction time (p. 48, left column, 3rd paragraph).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine teaching of Chockchaisawasdee and Tang and substitute α-amylase Thermamyl SC in Chockchaisawasdee teaching with Kleistase from Tang teaching for preparation of liquified cassava starch. One would have been motivated to do so since Tang describes processing of cassava starch for application in fermentation industry. A skilled artisan would have reasonably expected success in the combination because Chockchaisawasdee and Tang teach α-amylases for liquefaction of the starch. One would have been motivated to optimize parameters of Kleistase reaction to achieve complete starch liquefaction. A skilled artisan would have reasonably expected success in this optimization because optimization of the parameters of the enzymatic reaction is routine and conventional.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to assume that partial starch hydrolysis with α-amylase can reach DE of up-to 12 as was shown in Khatoon teaching and that hydrolysis with α-amylase can be applied to different starches including tapioca starch. One would have been motivated to do that since Khatoon teaches that α-amylase hydrolysis to several starches including tapioca starch results in decrease in solid properties of starches and presence of oligosaccharides with broad molecular weight distribution. A skilled artisan would have reasonably expected success in that because Chockchaisawasdee, Tang and Khatoon teach hydrolysis of starches with α-amylases.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to add Branchzyme from Lee teaching for preparation of liquified starch based on Chockchaisawasdee, Tang and Khatoon teachings. One would have been motivated to do so since Lee teaches that Branchzyme provides preparation of slowly digestible oligosaccharides. A skilled artisan would have reasonably expected success in the combination because of Chockchaisawasdee, Tang and Lee teach liquefaction of the starch prior to saccharification.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow Niu teaching and determine DE in the process of liquefaction of starch during enzymatic reactions of Kleistase and Branchzyme, described in teachings of Tang and Lee and achieve DE of 20 or higher after both reaction prior to saccharification as described by Niu. One would have been motivated to do so since Niu showed that increasing DE was beneficial to IMO formation increasing yields per reaction time. A skilled artisan would have reasonably expected success in the combination because Chockchaisawasdee, Tang, Lee, Niu and Khatoon teach hydrolysis of starch and Chockchaisawasdee and Niu describe preparation of IMO.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that parameters of reaction, such as the time of Fungamyl 800L reaction and inactivation of enzymes are the result effective variables. One would have been motivated to optimize the time of reaction and time for inactivation to reach starch saccharification and to stop enzymatic reactions, respectively. A skilled artisan would have reasonably expected success in this optimization because selection of reaction time and inactivation time is routine and conventional.
Thus, Chockchaisawasdee, Tang, Khatoon, Lee and Niu teachings render claim 1 obvious.
Regarding claim 2, Chockchaisawasdee teaches addition of 0.3 ml of Fungamyl 800L per 500 g of the slurry (p. 181, right column, 5th paragraph) that is close to claimed effective amount of 0.8 ml per kg of dry weight.
Regarding claim 3, Chockchaisawasdee teaches addition of 0.3 ml of Transglucosidase L per 500 g of the slurry (same as in the previous reaction since it was continuation step) (p. 182, left column, 1st paragraph) that is close to claimed effective amount of 1.4 ml per kg of dry weight.
The concentration and/or activity of Fungamyl 800L and Transglucosidase L from instant application and prior art are not defined and hence it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that the effective amount of Fungamyl 800L and Transglucosidase L in the prior art and claimed application can be the same or if it is not the same one would be motivated to optimize the amount of enzymes to reach starch saccharification. A skilled artisan would have reasonably expected success in this optimization because selection of amount of enzyme in the reaction is routine and conventional. Thus, Chockchaisawasdee, Tang, Khatoon, Lee and Niu teachings render claims 2 and 3 obvious.
Regarding claim 5, Tang teaches the effective amount of Kleistase of 0.3% (v/v) (p. 160, 3rd paragraph) and that makes 0.07% (v/w) taking into consideration 22.5% suspension as described above. That parameter is close to claimed 0.04% (v/w).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to optimize the amount of Kleistase from Tang teaching for liquefaction of the starch based on Chockchaisawasdee, Tang, Lee, Niu and Khatoon teachings. One would have been motivated to optimize the amount to achieve complete starch liquefaction. A skilled artisan would have reasonably expected success in this optimization because optimization of the amount of the enzyme in the reaction is routine and conventional. Thus, Chockchaisawasdee, Tang, Khatoon, Lee and Niu teachings render claim 5 obvious.
Regarding claim 6, Lee teaches the effective amount of Branchzyme, 500 U/g of dry weight of starch (p. 4, right column, 2nd paragraph), that is close to claimed 600 U/g dry weight of starch.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to optimize the amount of Branchzyme from Lee teaching for liquefaction of the starch based on Chockchaisawasdee, Tang, Lee, Niu and Khatoon teachings. One would have been motivated to optimize the amount to achieve complete starch liquefaction. A skilled artisan would have reasonably expected success in this optimization because optimization of the amount of the enzyme in the reaction is routine and conventional. Thus, Chockchaisawasdee, Tang, Khatoon, Lee and Niu teachings render claim 6 obvious.
Regarding claim 25, Lee teaches hydrolysis property of the modified starches by human pancreatic α-amylase followed by hydrolysis with mucosal α-glucosidases (p. 7, left column, last paragraph and right column, 1st paragraph). Lee discloses that hydrolysis showed the slow digesting property of the prepared starches (Abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow Lee teaching and test the resistance of IMO prepared based on Chockchaisawasdee, Tang, Lee, Niu and Khatoon teachings on human gut enzymes as described by Lee with α-amylase and α-glucosidase. One would have been motivated to do so since Lee showed that modification of the starch causes increase in the resistance to human gut enzymes when tested with pancreatic α-amylase and mucosal α-glucosidases. A skilled artisan would have reasonably expected success in the combination because Chockchaisawasdee, Lee and Niu teach preparation of modified oligosaccharides. Thus, Chockchaisawasdee, Tang, Khatoon, Lee and Niu teachings render claim 25 obvious.
Claims 7, 8, 12 and 13 are rejected under 35 U.S.C. 103 as being unpatentable over
Chockchaisawasdee (Chockchaisawasdee and Poosarah J. Sci. Food Agric., 2013, 93, 180-186) in view of Thang (Thang et al. Appl. Biochem. Biotechnol., 2010, 161, 157- 170), Khatoon (Khatoon et al. Food Res. Internat., 2009, 42, 1426-1433), Lee (Lee et al. PLOS One, 2013, 8, e59745, 1-10 on record in IDS) and Niu (Niu et al. Electronic J. Biotechn., 2017, 26, 46-51 on record in IDS) as applied to claim 1 above, and further in view Okada (US 20160177356 A1).
The teachings of Chockchaisawasdee, Khatoon, Thang, Lee and Niu have been set forth above.
Chockchaisawasdee, Khatoon, Thang, Lee and Niu do not teach preparation of IMO to include GlycoTransferase (GTase) prior to Fungamyl 800L reaction or after Fungamyl 800L reaction prior to Transglucosidase reaction.
Regarding claim 7 and 12, Okada teaches a method for producing an indigestible saccharide using novel glycotransferase, maltotriosyl transferase (paragraphs 0002 and 0005). Okada discloses that novel glycotransferase acts on a saccharide, preferably dextrin, obtained by action of α-amylase on the starch (paragraph 0090). Okada mentions different sources of starch including cassava starch and tapioca starch (paragraph 0090). Okada describes that glycotransferase (GTase) can be added before saccharification step or after saccharification step (paragraph 0096). The saccharification step is performed by Fungamyl 800L in Chockchaisawasdee teaching as described above and hence GTase from Okada teaching can be added either before Fungamyl 800L reaction or after. Regarding parameters of GTase reaction, Okada teaches the temperature of reaction of about 45°C to 55°C (paragraph 0056) and pH range of about 6.5 to 8.0 that covers claimed limitations. Okada mentions 1-3 hours of the time of the reaction during testing substrate specificity of GTase (paragraph 0138) and mentions stirring of the reaction in a mixer (paragraph 0145) that reads on claimed limitation for the time of reaction.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine teaching of Chockchaisawasdee and Okada and add GTase from Okada teaching as additional step in preparation of IMO based on Chockchaisawasdee, Tang, Khatoon, Lee and Niu teachings wherein that step can be added either before Fungamyl 800L reaction (as claimed in claim 7) or after Fungamyl 800L reaction (as claimed in claim 12). One would have been motivated to do so since Okada teaches preparation of indigestible, and hence resistant oligosaccharides. A skilled artisan would have reasonably expected success in the combination because Okada, Chockchaisawasdee, Thang, Khatoon, Lee and Niu describe methods of preparation of oligosaccharides from starch. Thus, Okada, Chockchaisawasdee, Tang, Khatoon, Lee and Niu teachings render claims 7 and 12 obvious.
Regarding claims 8 and 13, Okada teaches that the amount of added GTase: “is not particularly limited, and may be from 1 U to 400 U for 1 g of the substrate.” (paragraph 0095). Okada does not specify the amount of GTase in Units per ml of solution. However, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that the amount of the added enzyme is determined by the amount of its substrate and can be adjusted depending of the substrate concentration in the solution. One would have been motivated to optimize the amount of GTase to achieve maximal GTase activity in the required time of the reaction. A skilled artisan would have reasonably expected success in this optimization because Okada provides a wide range of the amount of GTase and optimization of the amount of the enzyme in the reaction is routine and conventional. Thus, Chockchaisawasdee, Tang, Khatoon, Lee, Niu and Okada teachings render claims 8 and 13 obvious.
Claims 9-11 and 14-17 are rejected under 35 U.S.C. 103 as being unpatentable over Chockchaisawasdee (Chockchaisawasdee and Poosarah J. Sci. Food Agric., 2013, 93, 180-186) in view of Thang (Thang et al. Appl. Biochem. Biotechnol., 2010, 161, 157- 170), Khatoon (Khatoon et al. Food Res. Internat., 2009, 42, 1426-1433), Lee (Lee et al. PLOS One, 2013, 8, e59745, 1-10 on record in IDS), Niu (Niu et al. Electronic J. Biotechn., 2017, 26, 46-51 on record in IDS) and Okada (US 201601777356 A1) as applied to claims 1, 12 above, and further in view of Zhou (Zhou et al. Carbohydrate Research, 2010, 345, 1752-1759).
The teachings of Chockchaisawasdee, Khatoon, Thang, Lee, Niu and Okada have been set forth above.
Chockchaisawasdee, Khatoon, Thang, Lee and Niu do not teach preparation of IMO to include Cycloglucanotransferase reaction.
Regarding claims 9, 14 and 15, Okada teaches addition of GTase either before saccharification reaction with Fungamyl 800L or after as described above. Okada teaches that combination of GTase and cyclodextrin glucanotransferase (CGTase) increases the formation of the indigestible/resistant oligosaccharide (paragraph 0094). Okada describes CGTase Toruzyme 3.0 L from Novozymes (paragraph 0094). Okada does not teach addition of CGTase of a separate step after Fungamyl 800L reaction (claim 9), after Fungamyl 800l and GTase reaction (claim 14) and after GTase reaction and before Fungamyl 800L reaction (claim 15).
Zhou teaches glycosylation with CGTase of Toruzyme 3.0 L and describes CGTase of Toruzyme 3.0 L as extremely thermophilic enzyme (Abstract). Zhou describes very broad pH activity range with high activity from pH 5 to 9 (p. 1756, left column, Figure 4). Zhou discloses the temperature dependence that showed increase in the activity of CGTase with increasing temperature and maximal activity at 100°C (p. 1756, left column, Figure 5) and the time course of the reaction demonstrating stable activity from 10 to 120 min (p. 1756, right column, Figure 7). Zhou mentions that starch, dextrin and maltose can be used in transglycosylation reaction of CGTase (p. 1756, right column, 1st paragraph).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to add CGTase from Okada and Zhou teaching as additional step in preparation of IMO described by combination of Chockchaisawasdee, Khatoon, Tang, Lee, Niu teachings wherein CGTase can be added as separate step since the reaction parameters of CGTase are different from those for Fungamyl 800L and GTase. It would have been obvious to try adding the CGTase step after Fungamyl 800L reaction, after Fungamyl 800l and GTase reaction or after GTase reaction and before Fungamyl 800L reaction to select the best protocol for IMO preparation. One would have been motivated to do so since Okada teaches preparation of indigestible, and hence resistant oligosaccharides using GTase and CGTase and Zhou teaches highly thermophilic CGTase. A skilled artisan would have reasonably expected success in the combination because Chockchaisawasdee, Khatoon, Tang, Lee, Niu, Okada and Zhou describe methods and enzymes for preparation and modification of oligosaccharides from starch. Thus, Chockchaisawasdee, Khatoon, Tang, Lee, Niu, Okada and Zhou teachings render claims 9, 14 and 15 obvious.
Regarding claims 10 and 16, Okada teaches the amount of added GTase in the range from 1 U to 400 U for 1 g of the substrate as described above (paragraph 0095). Okada does not specify the amount of GTase in Units per ml of solution. However, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that the amount of added enzyme is determined by the amount of its substrate and can be adjusted depending of the substrate concentration in the solution. One would have been motivated to optimize the amount to achieve maximal GTase activity in the required time of the reaction. A skilled artisan would have reasonably expected success in this optimization because Okada provides a wide range of the amount of GTase activity and optimization of the amount of the enzyme in the reaction is routine and conventional. Thus, Chockchaisawasdee, Khatoon, Tang, Lee, Niu, Okada and Zhou teachings render claims 10 and 16 obvious.
Regarding claims 11 and 17, Okada teaches that the amount of CGTase in the reaction is from 0.1 mg to 20 mg for 1 g of the substrate (paragraph 0094). Okada does not specify the activity of CGTase/Toruzyme 3.0 L. Zhou teaches the specific activity of CGTase from Toruzyme 3.0 L from 2.16 to 16.26 U/mg (p. 1756, Table 2). That covers claimed limitations for the effective amount of CGTase in claims 11 and 17.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow guidance of Okada and Zhou on the amount of CGTase in preparation of IMO described by combination of Chockchaisawasdee, Khatoon, Tang, Lee, Niu teachings. One would have been motivated to do so with reasonably expected success since Okada and Zhou teach application of the same CGTase, Toruzyme 3.0 L, for transglycosylation of saccharides and Chockchaisawasdee, Khatoon, Tang, Lee, Niu, Okada and Zhou describe methods and enzymes for preparation and modification of oligosaccharides from starch. Thus, Chockchaisawasdee, Tang, Khatoon, Lee, Niu, Okada and Zhou teachings render claims 11 and 17 obvious.
Response to Arguments
Applicant's arguments filed 08/07/2025 have been fully considered but they are not persuasive.
Applicant argues (addressing p. 18-19 of the Remarks) that Chockchaisawasdee, Thang, Lee and Niu do not teach all the limitations of the amended claim 1, specifically Chockchaisawasdee and Niu do not teach tapioca starch and digestion-resistant IMO. These arguments are not persuasive because:
In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). In instant case, amended claim 1 is rejected based on combination of prior art of Chockchaisawasdee, Tang, Khatoon, Lee and Niu as described in the rejection above. Chockchaisawasdee, Tang, Khatoon, Lee and Niu teach different limitations of claim 1, i.e. briefly, Chockchaisawasdee, Tang and Khatoon teach starch hydrolysis with α-amylases and Khatoon teaches hydrolysis of tapioca starch with DE reaching 12 (Abstract); Tang provides Kleistase as α-amylase (p. 160, 3rd paragraph), Lee teaches additional branching enzyme for liquefaction of starch (p. 4, left column, 3rd paragraph) and Niu teaches DE of more than 20 reached for liquified starch prior to production of IMO (p. 47, right column, 3rd paragraph), then Chockchaisawasdee teaches synthesis of IMO from liquified starch by treatment with a second α-amylase, Fungamyl 800L (p.181, left column, 2nd paragraph), and transglucosidase (Abstract).
In response to applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, one would have been motivated to use α-amylase Kleistase from Thang (p. 160, 3rd paragraph) instead of Thermamyl of Chockchaisawasdee (p. 181, left column, 2nd paragraph), since Kleistase is used for the same purpose of starch hydrolysis, and Branchzyme of Lee teaching (p. 4, left column, 3rd paragraph) since it provides slowly digestible oligosaccharides (Abstract). One would be motivated to follow Khatoon and Niu teachings and determine DE during starch hydrolysis for both enzymatic reactions of α-amylase Kleistase and branching enzyme Branchzyme and reach DE of about 12 for partial hydrolysis with Kleistase since Khatoon teaches that DE value correlates with decrease in solid properties of starches and presence of oligosaccharides with broad molecular weight distribution (Abstract) and reach DE of more than 20 for complete liquified starch since Niu showed that increasing DE was beneficial to IMO formation increasing yields per reaction time (p. 48, left column, 3rd paragraph)h. A skilled artisan would have reasonably expected success in combination of references because all of them are in the same filed of endeavor teaching modification of starch and Chockchaisawasdee and Niu describe production of IMO.
In response to Applicant’s arguments (addressing p. 18-19 of the Remarks), that Thang teaches cassava starch and not tapioca starch which is coming from the same yucca root but: “ is derived from a process called washing and pulping, where the root is grated and rinsed, leaving behind starchy water” and Thang teaching is directed to production of acetone-ethanol-butanol and not digestion-resistant IMO, these arguments are not persuasive because:
Although Thang describes the same process of preparation of cassava starch: “Extraction of starch from fresh cassava roots can be divided into five main stages: preparation (peeling and washing), rasping/pulping/grating, purification (starch washing), dewatering and drying, and finishing (milling and packaging).” (p. 159, 2nd paragraph), the current rejection is modified to incorporate the prior art of Khatoon, that teaches hydrolysis of several starches including tapioca starch (Abstract). Although Thang teaching is directed to production of acetone-ethanol-butanol, the raw material Thang is using is starch and preparation of liquified starch by α-amylase hydrolysis is the same as in Chockchaisawasdee teaching providing reasonably expected success in using α-amylase Kleistase of Thang teaching for starch liquification for IMO production.
In response to Applicant’s arguments (addressing p. 19 of the Remarks), that Lee is directed to resistant maltodextrin and not digestion-resistant IMO, these arguments are not persuasive because:
Although Lee teaches maltodextrin carbohydrates, Lee discloses that modification of starch with the branching enzyme provides digestion resistance (Abstract) and hence it is advantages to add this enzyme treatment during production of digestion-resistant IMO as well. Additionally, the recitation “for preparing a resistant-isomalto-oligosaccharide with digestion-resistance to human gut enzymes” can be interpreted as intended use. The intended use is given weight to the extent that it imparts a structural limitation and the prior art needs to be capable of performing the intended use. See MPEP 2111.02, section II. In instant case, the combination of prior art teaches the same instantly claimed method steps of preparing IMO and therefore, the method described in the combination of prior art of Chockchaisawasdee, Tang, Khatoon, Lee and Niu is capable of achieving the same goal of production of digestion-resistant IMO unless shown on the contrary.
In response to Applicant’s arguments (addressing p. 19 of the Remarks), that Chockchaisawasdee, Tang, Lee and Niu to do not teach, suggest, motivate or disclose the specific sequence and timing of multiple enzymes addition and application of CGTase and GTase in the claimed manner, these arguments are not persuasive because:
The teachings of Tang, Lee and Niu are applied for the step of preparing liquified starch, Chockchaisawasdee teaches preparation of IMO from liquified starch by action of the second α-amylase, Fungamyl 800L, and transglucosidase. Chockchaisawasdee, Tang, Lee and Niu do not teach CGTase and GTase, however one would have been motivated to add GTase from Okada teaching because Okada discloses that GTase produce indigestible saccharides (paragraphs 0002) and since Okada teaches that GTase can be added either prior or after saccharification (paragraph 0096), GTase treatment can be added either before Fungamyl 800L treatment or after. Okada teaches that addition of CGTase to GTase increases formation of indigestible saccharide (paragraph 0094) and Zhou teaches CGTase as extremely thermophilic enzyme (Abstract) that provides motivation to add CGTase to prepare digestion-resistance IMO and add CGTase in a separate step since its reaction parameters are different from those of Fungamyl 800L and GTase of Okada. One would be motivated to try different sequence of addition of these enzymes by adding the CGTase step after Fungamyl 800L reaction, after Fungamyl 800L and GTase reaction or after GTase reaction and before Fungamyl 800L reaction to select the best protocol for IMO preparation.
Thus, the 35 U.S.C. 103 rejection is maintained and modified necessitated by amendment of claims.
Conclusion
No claims are allowed.
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 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 LIOUBOV G KOROTCHKINA whose telephone number is (571)270-0911. The examiner can normally be reached Monday-Friday: 8:00-5:30.
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/L.G.K./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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