Prosecution Insights
Last updated: July 17, 2026
Application No. 18/568,085

SYSTEMS AND METHODS FOR SUGAR-REDUCTION AND/OR FIBER PRODUCTION FOR FOOD AND OTHER APPLICATIONS

Non-Final OA §102§103
Filed
Dec 07, 2023
Priority
Jun 08, 2021 — provisional 63/208,473 +1 more
Examiner
SWAIN, MARLA DANELLE
Art Unit
1793
Tech Center
1700 — Chemical & Materials Engineering
Assignee
Massachusetts Institute of Technology
OA Round
1 (Non-Final)
Grant Probability
Favorable
1-2
OA Rounds

Examiner Intelligence

Grants only 0% of cases
0%
Career Allowance Rate
0 granted / 0 resolved
-65.0% vs TC avg
Minimal +0% lift
Without
With
+0.0%
Interview Lift
resolved cases with interview
Typical timeline
Avg Prosecution
4 currently pending
Career history
4
Total Applications
across all art units

Statute-Specific Performance

§103
100.0%
+60.0% vs TC avg
Black line = Tech Center average estimate • Based on career data from 0 resolved cases

Office Action

§102 §103
DETAILED ACTION Notice of Pre-AIA or AIA Status The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA . Claim Status The status of the claims stands as follows: Pending claims: 1–7, 54–60 and 68–73 Claims currently under consideration: 1–7, 54–60 and 68–73 Currently rejected claims: 1–7, 54–60 and 68–73 Allowed claims: None Priority Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. Specification The abstract of the disclosure is objected to because the abstract does not adhere to the 150-word limit. A corrected abstract of the disclosure is required and must be presented on a separate sheet, apart from any other text. See MPEP § 608.01(b). Applicant is reminded of the proper content of an abstract of the disclosure. A patent abstract is a concise statement of the technical disclosure of the patent and should include that which is new in the art to which the invention pertains. The abstract should not refer to purported merits or speculative applications of the invention and should not compare the invention with the prior art. If the patent is of a basic nature, the entire technical disclosure may be new in the art, and the abstract should be directed to the entire disclosure. If the patent is in the nature of an improvement in an old apparatus, process, product, or composition, the abstract should include the technical disclosure of the improvement. The abstract should also mention by way of example any preferred modifications or alternatives. Where applicable, the abstract should include the following: (1) if a machine or apparatus, its organization and operation; (2) if an article, its method of making; (3) if a chemical compound, its identity and use; (4) if a mixture, its ingredients; (5) if a process, the steps. Extensive mechanical and design details of an apparatus should not be included in the abstract. The abstract should be in narrative form and generally limited to a single paragraph within the range of 50 to 150 words in length. See MPEP § 608.01(b) for guidelines for the preparation of patent abstracts. Claim Rejections – 35 USC § 102 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. Claims 54, 55, 56, 58 and 59 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Bongers et al. (US 2010/0136171 A1). Bongers et al. is directed to food products that contain “taste essential” [0031] carbohydrates associated with high caloric intake and adverse effects on human health [0001]. Bongers et al. teaches a food composition comprising at least one mono- and/or disaccharide and at least one microorganism and/or enzyme [0018] wherein the microorganism and/or enzyme is capable of converting (i.e., polymerizing) digestible mono- and/or disaccharides to non-digestible molecules such as glucose or fructose polymers [0043]. Bongers et al. also teaches an embodiment of the composition where the microorganism and/or enzyme component may be encapsulated in a solid matrix, including a gel-like matrix, and physically separated from the reactant mono- or disaccharides prior to consumption [0054]-[0055]. Further, Bongers et al. teaches a food composition where, prior to consumption, the microorganism and/or enzyme and the mono- and/or disaccharide sugar do not react due to the presence of a reversible inhibitor or other chemical conditions, such as non-optimal pH or temperature [claims 9 and 10]. Regarding claim 55, Bongers et al. teaches all of the elements of claim 54 as described above. In addition, Bongers et al. teaches an embodiment where “the taste essential” carbohydrate ingredient is selected from sucrose, fructose, lactose, galactose and maltose [0032]. Regarding claim 56, Bongers et al. teaches all of the elements of claim 54. In addition, Bongers et al. teaches that commonly used “taste essential” carbohydrates such as sucrose, maltose and fructose are converted to indigestible molecules such as fructo- and gluco-oligosaccharides [0043]. Regarding claim 58, Bongers et al. teaches all of the elements of claim 54. Bongers et al. also teaches that suitable enzyme components of the food composition are glucosyltransferases, fructosyltransferases and galactosyltransferases [0047], all of which are categorized as glycosyltransferases. Regarding claim 59, Bongers et al. teaches all of the elements of claim 58. In addition, Bongers et al. teaches that the food composition comprises an enzyme (and/or a microorganism that produces an enzyme) selected from a group that includes inulosucrase, levansucrase [0047] and sucrase [0041]. 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. This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claims 1-4 are rejected under 35 U.S.C 103 as being unpatentable over Bongers et al. as evidenced by Copeland (Copeland, R. A. Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis, 2nd ed.; Wiley-VCH: New York, 2000) and Zhou et al. (Zhou, H. et al. Chem Rev., 2018, 118:1691–1741 [doi:10.1021/acs.chemrev.7b00305]). Regarding claim 1, Bongers et al. teaches a food composition comprising a microorganism and/or an enzyme and mono- or disaccharides [0016], where the microorganism and/or enzyme is capable of polymerizing sugars [0060]. Bongers et al. also teaches that the microorganism and/or enzyme may be encapsulated in a solid matrix, incorporated into an emulsion or double emulsion, or a combination thereof, to prevent interactions with mono- and disaccharides in the food composition prior to consumption [0054-0057]. Regarding the limitation in the instant claim that the particle composition comprises an inhibitor that is associated with the enzyme, Bongers et al. teaches that the composition may comprise a reversible inhibitor to the enzyme to prevent enzyme-sugar interactions that result in the polymerization of sugars in the food composition prior to consumption so that the food composition retains its taste or mouthfeel when consumed [claims 9 and 10]. Bongers et al. also teaches that the invention starts to act in the stomach resulting in a higher amount of digestible sugars being converted to compounds (i.e., non-digestible oligosaccharides) [0029], compared to the amount of non-digestible oligosaccharide compounds that would be produced if the composition was initially activated in the intestines where digestible sugars are quickly absorbed [0015]. Finally, Bongers et al. discloses that the microorganism and/or enzyme of the composition are active at the temperature (i.e., about 37 °C) and pH range of the stomach (i.e., between pH 5 and 7, upon ingestion of the food composition, and between pH 2-4 as digestion progresses) [0027]. While Bongers et al. does not specifically teach an enzyme and inhibitor that dissociates at the recited pH and ionic strength, it would have been obvious for an enzyme and an associated inhibitor that inhibits the enzyme from polymerizing sugars to dissociate under particular reaction conditions such as those cited in the instant claim (i.e., ionic strength of at least 5 mmol/L and pH greater than 3.5). As stated above, Bongers et al. teaches a food composition comprising an enzyme and mono- and disaccharides that may also include an inhibitor. Bongers et al. also teaches that the enzyme that polymerizes sugars should be active at pH ranges comparable to stomach pH after food is consumed (i.e., pH ranges from 2 to 7), which indicates that an embodiment of the food composition comprising an enzyme bound to an inhibitor will undergo inhibitor dissociation at stomach pH ranges so that the enzyme can polymerize sugars. In addition, the claimed enzyme-inhibitor interaction (i.e., dissociation), which is limited by pH and ionic strength conditions in the instant claim, is an inherent property of the enzyme-inhibitor particle composition. Since the food composition of Bongers et al. reads on the composition recited in the instant claim, the functional characteristic of enzyme-inhibitor dissociation under specific pH and ionic strength is also inherently present in the prior art composition. It is well established in the art that noncovalent, reversible enzyme-inhibitor interactions are mediated by weak, electrostatic interactions such as hydrophobic and ionic interactions, hydrogen bonding, and Van der Waals forces (Copeland, p. 32-36, § 2.4) and that these interactions, and the related enzyme activity, are intrinsically associated with reaction conditions such as temperature, pH, and ionic strength (Copeland, p. 121, ¶ 5). Specifically, it is commonly known in the art that increasing the ionic strength of an enzyme-inhibitor solution induces shielding of charges that are involved in electrostatic interactions leading to weakened noncovalent enzyme-inhibitor bonding. The inherent association of noncovalent enzyme-inhibitor interactions and ionic strength is well known in the art and is exploited in separation techniques such as ion exchange chromatography (Copeland, p. 229, ¶ 4). In addition, it is commonly known in the art that altering the pH of an enzyme solution away from the enzyme’s optimal pH range of activity (i.e., pH range of maximum catalytic efficiency) may lead to protonation/deprotonation of side-chain residues within the active site and result in changes in enzyme-inhibitor interactions (Zhou et al., p. 2, ¶ 4 and p. 3, ¶ 1). It is also well known in the art that pH concentrations of an enzyme solution can affect enzyme tertiary and secondary structure, leading to enzyme denaturation and possible precipitation at extremely high and low pH (Copeland, p. 241, ¶ 3). One of ordinary skill in the art would recognize that the noncovalent, reversible binding interactions disclosed in Bongers et al. are a necessary consequence of the nature of the enzyme-inhibitor composition. The inherency of such functional characteristics of enzymes is further evidenced by Copeland where it is noted that native enzymes are optimally stabilized by certain solution conditions (i.e., pH, ionic strength and anion/cation composition), and that the optimal conditions for each enzyme must be determined experimentally (p. 258, ¶ 3). Regarding claims 2, 3 and 4, all of the elements of claim 1 are taught as described above. As for the ionic strengths recited in the instant claims 2, 3 and 4 (i.e., at least 10 mM, 25 mM and 50 mM, respectively), Bongers et al. does not teach embodiments of an enzyme-inhibitor particle composition having the recited ionic strengths. However, as previously stated with respect to claim 1, the functional characteristics of an enzyme and the enzyme’s interactions with an inhibitor are inherent. Further, native enzymes are optimally stabilized by reaction conditions such as pH, ionic strength and anion/cation compositions, and the optimal reaction conditions for enzyme catalysis must be determined experimentally (Copeland, p. 258, ¶ 3). Claims 5 and 6 are rejected under 35 U.S.C. as being unpatentable over Bongers et al. as evidenced by Copeland and Zhou et al. as applied to claim 1, and further in view of Incani et al. (Incani, V. et al. Cellulose, 2013, 20:191–200) as evidenced by Aeron et al. (Aeron, G. et al. Adv. Res. Biotech, 2017, 2(3): 1-4. [DOI: http://dx.doi. org/10.15226/2475-4714/2/3/00129]). Regarding claim 5, all of the elements of claim 1 are taught as described above. Bongers et al. does not teach a food particle composition comprising an enzyme and inhibitor where the enzyme is attached to a substrate. However, Incani et al. teaches an enzyme nanocomposite prepared by treating a nanocrystalline cellulose (NCC) colloidal suspension with polyethyleneimine (PEI) followed by the addition of gold nanoparticles (AuNP) to produce an NCC/PEI/AuNP nanocomposite (p. 193, ¶ 2–4). Incani et al. also teaches that the resulting nanocomposite is then incubated with 11-mercaptoundecanoic acid (MUDA) to produce a thiol modified nanocomposite, which is a substrate according to the instant specification (p. 21, ll. 15–17). Further, Incani et al. teaches the use of EDC/NHS coupling to covalently immobilize the enzyme glucose oxidase (GOD) to produce NCC/PEI/AuNP-S-(MUDA)-NHGOD (p. 193, ¶ 5). It would have been obvious for one of ordinary skill in the art to attach the enzyme of an enzyme-inhibitor particle composition to a substrate. While Bongers et al. does not teach the attachment of an enzyme to a substrate, Bongers et al. does teach an embodiment of a food composition where the enzyme component is encapsulated or incorporated into a solid matrix to limit enzyme-sugar interactions before the food composition is consumed. Encapsulating an enzyme is considered to be a type of immobilization (Aeron et al., p. 1, ¶4) and one of ordinary skill in the art would have been motivated to use alternative methods of immobilization to extend the applicability of the instant enzyme-inhibitor particle composition. Incani et al. teaches an enzyme immobilization strategy with the objective of preventing enzymes from being released into solution (p. 196, ¶ 4). Therefore, it would have been obvious to use the immobilization strategy of Incani et al. to modify the composition of Bongers et al., rendering the attachment of the enzyme component of the composition to a substrate as recited in the instant claim obvious. Regarding claim 6, all of the elements of claim 5 are taught as described above. Bongers et al. does not teach an enzyme-inhibitor particle composition where the enzyme is attached to a substrate comprising nanocellulose. However, as discussed with respect to claim 5, Incani et al. teaches the attachment of GOD to a nanocomposite comprised of nanocrystalline cellulose. (p. 193, ¶ 5). The rationale used to the support the obviousness of the attachment of the enzyme of an enzyme-inhibitor composition to a substrate, with respect to claim 5, may similarly be applied to the instant claim. In brief, Bongers et al. does not teach the attachment of an enzyme of a particle composition to a nanocellulose substrate, but does teach immobilization of an enzyme in a solid or gel-type matrix [0055]. One of ordinary skill in the art would have been motivated to consider alternative types of immobilization methods, depending on the final use of the composition (i.e., use for producing industrial polymers, biosensors, or therapeutic agents etc.). It would have been obvious for one of ordinary skill in the art to modify the immobilization method of Bongers et al., by incorporating the method of Incani et al. Therefore, the claim limitation of the substrate comprising nanocellulose recited in the instant claim would also have been obvious. Claim 7 is rejected under 35 U.S.C. as being unpatentable over Bongers et al., in view of Incani et al. as evidenced by Copeland, Zhou et al., and Aeron et al. as applied to claim 5, and further in view of Hussin et al. (Mohd-Hussin, F.N.N. et al. Enzyme and Microb. Technol., 2020, 136, 109505). Regarding claim 7, all of the elements of claim 5 are taught as described above. Bongers et al. does not teach a particle composition comprising an enzyme and inhibitor where the enzyme is attached to a substrate via a polymer. However, Hussin et al. teaches the use of an optimized immobilization method to irreversibly immobilize the digestive enzyme lipase to an alginate/nanocellulose/montmorillonite (ALG/NC/MMT) composite (p. 3, § 2.7). Hussin et al. also teaches that the nanocellulose component of the composite has a high surface area for increased enzyme loading and surface reaction activity (p. 1, ¶ 1), and that the immobilized enzyme has improved catalytic activity (p. 6, § 3.3) and thermal stability (p. 9, § 3.5.1) compared to the free (i.e., soluble) enzyme. Further, Hussin et al. discloses that the immobilized enzyme maintained about 50% of its initial activity for up to 9 cycles (p. 10, § 3.5.2). It would have been obvious to one of ordinary skill in the art to attach the enzyme component of an enzyme-inhibitor particle composition to nanocellulose using a polymer. While Bongers et al. does not specifically teach the attachment of the enzyme component of an enzyme-inhibitor complex to a substrate via a polymer, Bongers et al. does disclose the immobilization of the enzyme component through encapsulation or incorporation of the enzyme component into a solid or gel-like matrix [0055]. One of ordinary skill in the art would have been motivated to use alternative methods to improve the stability and catalytic activity of the enzyme. Therefore, it would have been obvious use the methods of Hussin et al. (i.e., attaching an enzyme to nanocellulose substrate treated with the polymer PEI) to produce a modified food composition of Bongers et al. Therefore, the instant claim limitation of attaching an enzyme via substrate via a polymer would also have been obvious. Claim 57 is rejected under 35 U.S.C. as being unpatentable over Bongers et al. as applied to claim 54, and in view of Nakahara et al. (Nakahara, K. et al. Appl. Environ. Microbiol. 1993, 59:4, 968-973). Regarding claim 57, all of the elements of claim 54 are taught by Bongers et al.as described above. Bongers et al. does not teach an enzyme-inhibitor composition where the inhibitor specifically comprises a polyphenol. However, Nakahara et al. teaches the effect of polyphenols derived from oolong tea extract on enzyme polymerization by glucosyltransferase I produced by the mutant Streptococcus sobrinus 6715 (abstract). Nakahara et al. also teaches that the polyphenols extracted from oolong tea significantly inhibited the catalytic activity of some types glucosyltransferases from mutans streptococci (p. 927, ¶ 2). It would have been obvious to one of ordinary skill in the art for the inhibitor in an enzyme-inhibitor composition to comprise a polyphenol. While Bongers et al. does not specifically teach a polyphenol inhibitor, Bongers et al. does teach that the enzyme of the food composition may be bound to a reversible inhibitor to prevent polymerization of sugar by the enzyme before ingestion (claims 9 and 10). One of ordinary skill in the art would have been motivated to consult a reference regarding compounds that inhibit an enzyme such as glucosyltransferase. Since Nakahara et al. teaches the inhibition of glucosyltransferase mediated sugar polymerization, it would have been obvious to use the polyphenol inhibitors of Nakahara et al.to produce the enzyme-inhibitor composition of Bongers et al. Therefore, it would have been obvious to have a particle composition where the inhibitor comprises a polyphenol, as recited in the instant claim. Claim 60 is rejected under 35 U.S.C. as being unpatentable over Bongers et al. as applied to claim 54, in view of Fu et al. (Fu, J. et al. J. Electroanal. Chem., 2015, 783, 92-99), as evidenced by Aeron et al. Regarding claim 60, all of the elements of claim 54 are taught as described above. Bongers et al. does not teach an enzyme-inhibitor particle composition where the enzyme component of the composition is attached to a substrate. However, Fu et al. teaches the irreversible adsorption of biomolecules to carboxymethyl cellulose (CMC) modified cellulose to overcome enzyme stability issues encountered by covalent coupling methods that result in loss of enzyme activity (p. 92, ¶ 2). Specifically, Fu et al. teaches the adsorption of CMC to cellulose nanofibers (CNF) that are then complexed with silver nanoparticles (AgNPs) to form an AgNPs-CMC-CNF conjugate that is then modified with the enzyme laccase to detect catechol, a polyphenol (p. 93, ¶ 1). It would have been obvious to one of ordinary skill in the art to attach the enzyme of a composition comprising an enzyme and an associated polyphenol to a substrate. As stated previously, Bongers et al. does not teach the immobilization of an enzyme to a substrate, but does teach encapsulation of an enzyme, which is considered to be a specific type of immobilization (Aeron, p. 1, ¶ 5). One of ordinary skill in the art would have been motivated to consult additional references directed to other enzyme immobilization methods that enhance catalytic activity. Since Fu et al. is directed to investigating the activity of an enzyme immobilized to CMC-CNF substrate, it would have been obvious to one of ordinary skill in the art to use the methods of Fu et al. to modify the methods Bongers et al. Therefore, it would have also been obvious to attach the enzyme of an enzyme-polyphenol composition to a substate, thus rendering the instant claim obvious. Claim 68 is rejected under 35 U.S.C. as being unpatentable over Bongers et al. in view of Nakahara et al. Regarding claim 68, Bongers et al. does not teach an enzyme-polyphenol food composition. However, as explained above, Nakahara et al. teaches that polyphenols extracted from oolong tea significantly inhibited the catalytic activity of some types glucosyltransferases from mutans streptococci (p. 927, ¶ 2). The rationale used to support the obviousness, with respect to claim 57, may similarly be applied to the instant claim. Briefly, Bongers et al. does not teach a specifically teach a food composition comprising and enzyme and an associated polyphenol. However, Bongers et al. does teach that an enzyme may be bound to a reversible inhibitor to prevent enzyme mediated polymerization of sugar prior to ingestion (claims 9 and 10). One of ordinary skill in the art would have been motivated to consult references for information on potential inhibitors to a particular enzyme that would ensure the stability of the composition prior its use (i.e., before ingestion). Since, Nakahara et al. discloses polyphenol inhibitors to the enzyme laccase (i.e., an enzyme listed in the instant claim), it would have been obvious to use the methods of Nakahara et al., and incorporate the use of a polyphenol inhibitor to the food composition of Bongers et al., thus rendering the instant claim obvious. Claim 69 is rejected under 35 U.S.C. as being unpatentable over Bongers et al. in view of Nakahara et al., as applied to claim 68, and further in view of Zhang et al. (Zhang, S. et al. Appl. Mater. Interfaces, 2015, 7 19570-15978, [DOI: 10.1021/acsami.5b03823). Regarding claim 69, all of the elements of claim 68 are taught as described above. Bongers et al. does not teach a composition where one or more enzymes of a particle composition is glucose oxidase (GOD), an enzyme capable of converting a glucose to gluconic acid. However, Zhang et al. teaches a microcapsule prepared by using CaCO3 as a template (p. 19571, § 1) to produce CaCO3 microspheres doped with poly(sodium 4-styrenesulfonate) (PSS) (PSS-CaCO3) that are then reacted with tannic acid (TA) to produce TA-coated CaCO3 microspheres (p. 19571, § 2.2). The resulting TA-coated CaCO3 microspheres are reacted with polyethyleneimine (PEI) to cross-link the TA coating (i.e., TA/PEI-CaCO3) and the CaCO3 template is removed to produce the TA/PEI microcapsules (p. 19571, § 2.2) that are reacted with glucose oxidase (GOD) to produce GOD-encapsulated TA/PEI microcapsules (p. 19571, § 2.5). It would have been obvious to one of ordinary skill in the art to produce an enzyme-polyphenol composition comprising the enzyme GOD. While Bongers et al. does not teach a food composition comprising the enzyme GOD, Bongers et al. is directed to regulating sugar to address adverse health effects ([0001] and [0002]). One of ordinary skill in the art would have been motivated to research other enzymes involved in regulating sugar in the diet. Zhang et al. teaches the immobilization of GOD and an assay to measure the catalytic activity of the encapsulated GOD in the microcapsule by monitoring H2O2 produced by the oxidation of β-glucose to gluconic acid (p. 19572, § 2.5). Since Zhang et al. teaches the use of GOD, an enzyme also involved in glucose regulation, it would have been obvious to use the enzyme of Zhang et al. to modify the food composition of Bongers et al. Therefore, the use of glucose oxidase, as the enzyme component of the particle composition in the instant claim would also have been obvious. Claims 70 and 71 are rejected under 35 U.S.C. as being unpatentable over Bongers et al. in view of Nakahara et al. and Fu et al., as evidenced by Aeron et al. Regarding claim 70, all of the elements of claim 68 are taught as described above. Bongers et al. does not teach a food composition comprising an enzyme that is attached to a substrate. However, as described above, Fu et al. teaches the attachment of the enzyme laccase to modified CMC-CNF (i.e., laccase-AgNPs-CMC-CNF (p. 93 and 94, §§ 2.2-2.4). The rationale to support the obviousness, with respect to claim 60, can be applied to the instant claim. Bongers et al. teaches a food composition where the enzyme (i.e., glucosyl-transferase) [0048], may be encapsulated in an emulsion [0057]. Since an encapsulation is a specific type of immobilization (Aeron, G. et al., p. 1, ¶ 4), one of ordinary skill in the art would have been motivated to research alternative methods of enzyme immobilization. Therefore, it would have been obvious to one of ordinary skill to use the immobilization methods of Fu et al. to make a modified food composition of Bongers et al., rendering the instant claim obvious. Regarding claim 71, all of the elements of claim 70 are taught as described above. Bongers et al. does not teach a food composition where the enzyme component is attached to a nanocellulose substrate. As discussed above, with respect to claim 70, Fu et al. teaches the immobilization of laccase to AgNPs-CMC-CNF (abstract). The rationale used to support the obviousness, with respect to claim 70, can similarly be applied to the instant claim. Since Bongers et al. and Fu et al. are directed to enzyme immobilization, it would have been obvious to one of ordinary skill in the art to use the method of Fu et al. to modify the immobilization method of Bongers et al. Therefore, it would also have been obvious to attach the enzyme component of a particle composition to a nanocellulose substrate, rendering the instant claim obvious. Claims 72 and 73 are rejected under 35 U.S.C. as being unpatentable over Bongers et al. in view of Nakahara et al., Fu et al.,, and Hussin et al. as evidenced by Aeron et al. Regarding claim 72, all of the elements of claim 70 are taught as described above. Bongers et al. does not teach a particle composition where the enzyme is attached to the substrate via a polymer. However, as described above, Hussin et al. teaches an optimized immobilization method to attach the digestive enzyme lipase to an ALG/NC/MMT composite (p. 3, § 2.7). The rationale used to support obviousness, with respect to claim 7, can similarly be applied to the instant claim. Briefly, since Bongers et al. discloses the immobilization of the enzyme (i.e., glycosyltransferase) component of a food composition by encapsulation, one of ordinary skill in the art would have been motivated to consult a reference directed to immobilization of enzymes u via a polymer. Since Hussin et al. teaches the immobilization of lipase to a nanocellulose substate that is modified with the polymer alginate, it would have been obvious to one of ordinary skill in the art to use the method of Hussin et al. to modify the immobilization strategy of Bongers et al. Therefore, the attachment of one or more enzymes to a substrate via a polymer would also have been obvious. Regarding claim 73, all of the elements of claim 72 are taught as described above. Bongers et al. does not teach a particle composition comprising an enzyme is attached to a substrate via the polymer carboxymethyl cellulose (CMC). It would have been obvious to use CMC as a polymer in the immobilization of an enzyme of a food composition. As discussed above, with respect to claim 70, Fu et al. teaches the immobilization of laccase to AgNPs-CMC-CNF (abstract) and teaches the improved catalytic activity and thermal stability attributed to immobilization of the enzyme. Since Bongers et al. is directed to the use of immobilizing enzymes through encapsulation, one of ordinary skill in the art would have been motivated to consult a reference directed to optimizing enzyme stability and activity through immobilization. Therefore, it would have been obvious to attach the enzyme of the food composition of Bongers et al. to a substrate via the polymer, CMC, thus rendering the instant claim obvious. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARLA SWAIN whose telephone number is 571-272-7095. The examiner can normally be reached 8:00 am–500 pm Eastern Time Monday-Friday. 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, Emily Le can be reached at 571-272-0903. 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. /MDS/Examiner, Art Unit 1793 /EMILY M LE/Supervisory Patent Examiner, Art Unit 1793
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Prosecution Timeline

Dec 07, 2023
Application Filed
Jul 07, 2026
Non-Final Rejection mailed — §102, §103 (current)

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