IP Library Granted Patent US 12,685,317
Granted Patent B2
US 12,685,317 · App. 18/026,395 · Granted Jul 21, 2026

Combination of nonmaltogenic exoamylase and glucoamylase for improving bread resilience and reducing amount of added sugars

Inventors: Jacob Flyvholm Cramer (Højbjerg, DK); Morgan Louise Gifford (Merriam, KS); Svend Haaning (Galten, DK); Lene Kragh (Højbjerg, DK); Vinni Høyer Lillelund (Bjerringbro, DK); Donald E. Ward (Overland Park, KS)
Assignee: INTERNATIONAL N&H DENMARK APS
A21D8/042C12N9/2414C12N9/2428C12Y302/01001C12Y302/01003
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Quick Facts
Patent No.
US 12,685,317
App. No.
18/026,395
Filed
Mar 15, 2023
Granted
Jul 21, 2026
Kind
B2
Art Unit
1791
USPC
426/18
Abstract

This invention relates to polypeptides, more specifically non-maltogenic alpha-amylase and glucoamylase polypeptides, and their uses in providing baked products with enhanced resilience.

Claims (6)

1 . A process for making a baked product with improved resilience, comprising adding to a dough comprising flour, water and a leavening agent, a nonmaltogenic exoamylase, wherein said nonmaltogenic exoamylase is an enzyme having at least 70%, 80%, 85%, 90%, 95%, 98%, 99% or 100% sequence identity to SEQ ID NO:1 or SEQ ID NO:2 and is present in an amount from about 15,000 to about 40,000 Betamyl Units per Kg of flour, and a glucoamylase, wherein said glucoamylase is an enzyme having at least 70%, 80%, 85%, 90%, 95%, 98%, 99% or 100% sequence identity to SEQ ID NO:3 and is present in an amount from about 5,000 to about 10,000 amyloglucosidase activity units (AGU) per Kg of flour, and baking the dough, wherein improved resilience means an increase in resilience measured as TPA resilience (A2/A1) relative to a corresponding baked product without the added nonmaltogenic exoamylase and glucoamylase under otherwise identical conditions.

2 . The process of claim 1 further comprising adding a third enzyme selected from the group of consisting of oxidoreductases, hydrolases, lipases, esterases, glycosidases, amylases, maltogenic alpha-amylases, pullulanases, xylanases, cellulases, hemicellulases, starch degrading enzymes, proteases and lipoxygenases.

3 . A dough comprising flour, a non-maltogenic exoamylase, wherein the nonmaltogenic exoamylase is an enzyme having at least 70%, 80%, 85%, 90%, 95%, 98%, 99% or 100% sequence identity to SEQ ID NO:1 or SEQ ID NO:2 and is present in an amount from about 15,000 to about 40,000 Betamyl Units per Kg of flour, and a glucoamylase, wherein the glucoamylase is an enzyme having at least 70%, 80%, 85%, 90%, 95%, 98%, 99% or 100% sequence identity to SEQ ID NO:3 and is present in an amount from about 5,000 to about 10,000 amyloglucosidase activity units (AGU) per Kg of flour.

4 . The dough of claim 3 further comprising a third enzyme selected from the group of consisting of oxidoreductases, hydrolases, lipases, esterases, glycosidases, amylases, maltogenic alpha-amylases, pullulanases, xylanases, cellulases, hemicellulases, starch degrading enzymes, proteases and lipoxygenases.

5 . The dough of claim 4 wherein the third enzyme is a maltogenic alpha-amylase.

6 . The dough of claim 5 which has been baked.

Assignments (2)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Apr 10, 2026
From: CRAMER, JACOB FLYVHOLM; KRAGH, LENE; LILLELUND, VINNI HOYER; GIFFORD, MORGAN; WARD, DONALD E.; HAANING, SVEND
To: DUPONT NUTRITION BIOSCIENCES APS
Reel/Frame 074334/0397 →
CHANGE OF NAME Recorded Feb 6, 2024
From: DUPONT NUTRITION BIOSCIENCES APS
To: INTERNATIONAL N&H DENMARK APS
Reel/Frame 066494/0814 →
Continuity (2)
Provisional Application 63080984 · Sep 21, 2020
Related Publication 20230404088A1 · Dec 21, 2023
References Cited (27)
US 5281526A · Good et al. · 1994 [cited by applicant]
US 6022725A · Fowler et al. · 2000 [cited by applicant]
US 20090202675A1 · Derkx et al. · 2009 [cited by applicant]
US 20090214706A1 · Berg · 2009 [cited by examiner]
US 20110136197A1 · Dodge et al. · 2011 [cited by applicant]
US 20120164695A1 · Aehle · 2012 [cited by examiner]
US 20120190075A1 · Kragh · 2012 [cited by examiner]
US 20180242598A1 · Feng et al. · 2018 [cited by applicant]
EP 0238023B1 · 1993 [cited by applicant]
WO 199117243A1 · 1991 [cited by applicant]
WO 199950399A2 · 1999 [cited by applicant]
WO 2005001036A2 · 2005 [cited by applicant]
WO 2011127802A1 · 2011 [cited by applicant]
WO 2016138315A1 · 2016 [cited by applicant]
WO 2018151185A1 · 2018 [cited by applicant]
WO 2018164737A1 · 2018 [cited by applicant]
Campbell et al, “Improved transformation efficiency of Aspergillus niger using the homologous niaD gene for nitrate reductase”, Curr Genet, vol. 16, 1989, pp. 53-56. [cited by applicant]
Cao et al, “Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to kcat”, Protein Science, vol. 9, 2000, pp. 991-1001. [cited by applicant]
Database GenBank [Online] 2002, Nielsen BR et al: “glucoamylase [Rasamsonia emersonii]”, XP55872425, Database accession No. CAC28076.1. [cited by applicant]
FGSC, Catalogue of Strains, University of Missouri, at www.fgsc.net (last modified Jan. 17, 2007). [cited by applicant]
Gornall et al, “Determination of serum proteins by means of the biuret reaction”, J Biol Chem., Feb. 1949, vol. 177, No. 2, pp. 751-766. [cited by applicant]
Harrison et al, “Employing Site-Specific Recombination for Conditional Genetic Analysis in Sinorhizobium meliloti”, Applied and Environmental Microbiology, vol. 77, No. 12, Jun. 2011, pp. 3916-3922. [cited by applicant]
International Search Report from PCT App. No. PCT/US2021/051241 dated Dec. 23, 2021, 5 pages. [cited by applicant]
Liu et al, “Improved heterologous gene expression in Trichoderma reesei by cellobiohydrolase I gene (cbh1) promoter optimization”, Acta Biochim. Biophys. Sin (Shanghai), vol. 40, No. 2, 2008, pp. 158-165. [cited by applicant]
Te'o et al, “Biolistic transformation of Trichoderma reesei using the Bio-Rad seven barrels Hepta Adaptor system”, Journal of Microbiological Methods, vol. 51, 2002, pp. 393-399. [cited by applicant]
Thompson et al., “Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice”, Nucleic Acids Research, 1994, vol.… [cited by applicant]
Weichselbaum, “An Accurate and Rapid Method for the Determination of Proteins in Small Amounts of Blood Serum and Plasma”, American Journal of Clinical Pathology, Mar. 1946, vol. 16, Issue 3, pp. 40-49. [cited by applicant]