IP Library Granted Patent US 12,661,389
Granted Patent B2
US 12,661,389 · App. 18/755,419 · Granted Jun 23, 2026

Use of low pH active alpha-1,4;/1,6-glycoside hydrolases (GLCH) as a feed additive for ruminants to enhance starch digestion

Inventors: Shukun Yu (Malmo, SE); Karsten Matthias Kragh (Hoejbjerg, DK); Wenting Li (Wiltshire, GB)
Assignee: INTERNATIONAL N&H DENMARK APS
A61K38/47A23K20/189A23K50/10A61K38/45A61K38/48A61K38/51A61K38/52A61P1/14
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Quick Facts
Patent No.
US 12,661,389
App. No.
18/755,419
Granted
Jun 23, 2026
Kind
B2
Abstract

Disclosed are uses of at least one alpha-1,4/1,6-glycoside hydrolase (GLCH) as a feed additive for a ruminant wherein said hydrolase: (a) has at least 20% activity at pH less than or equal to 3 in the presence of pepsin as compared to activity of the hydrolase at pH 6 in the presence of pepsin, (b) said hydrolase is active in at least two of three digestive chambers of a ruminant comprising a rumen, an abomasum and a small intestine and (c) the hydrolase works with pancreatic amylase to increase glucose yield.

Claims (16)

1 . A method for increasing starch digestibility and glucose yield in a ruminant which comprises:

(a) adding at least one fungal glucoamylase as a feed additive to feed for a ruminant,

wherein the at least one fungal glucoamylase is an EC 3.2.1.3 enzyme derived from Trichoderma reesei and:

(i) has at least 20% activity at pH less than or equal to 3 in the presence of pepsin as compared to activity of the hydrolase at pH 6 in the presence of pepsin;

(ii) is active in at least two of the three digestive chambers of a ruminant comprising a rumen, an abomasum, and a small intestine;

(iii) works with digestive enzymes present in the digestive chambers of the ruminant to increase starch digestibility and glucose yield; and

(iv) has at least 20% catalytic activity on maltose; and

(b) administering said feed additive to the ruminant, wherein starch digestibility and glucose yield in the ruminant is increased by said addition.

2 . The method of claim 1 wherein the at least one glucoamylase enzyme is capable of hydrolyzing raw starch under conditions comparable to those found in the rumen or abomasum.

3 . The method of claim 1 , further comprising adding at least one EC 3.2.1.1 alpha-amylase to the feed.

4 . The method of claim 3 , further comprising adding at least one xylanase to the feed.

5 . The method of claim 1 , further comprising adding at least one protease to the feed.

6 . The method of claim 5 wherein the protease is selected from the group consisting of an acid protease and a neutral metalloprotease.

7 . The method of claim 6 wherein the protease is a fungal aspartic protease or a bacterial neutral metalloprotease.

8 . The method of claim 5 , further comprising adding at least one xylanase to the feed.

9 . The method of claim 1 , further comprising adding at least one xylanase to the feed.

Continuity (3)
Continuation 16334586
Provisional Application 62398741 · Sep 23, 2016
Related Publication 20240424068A1 · Dec 26, 2024
References Cited (38)
US 5231017A · Lantero et al. · 1993 [cited by applicant]
US 6352851B1 · Nielsen et al. · 2002 [cited by applicant]
US 7354752B2 · Dunn-Coleman et al. · 2008 [cited by applicant]
US 7413879B2 · Dunn-Coleman et al. · 2008 [cited by applicant]
US 8945889B2 · Ge et al. · 2015 [cited by applicant]
US 20030165478A1 · Sokoll · 2003 [cited by applicant]
US 20050037053A1 · Isaksen et al. · 2005 [cited by applicant]
US 20060094080A1 · Dunn-Coleman et al. · 2006 [cited by applicant]
US 20150147786A1 · Clarkson et al. · 2015 [cited by applicant]
US 20150376668A1 · Ge et al. · 2015 [cited by applicant]
US 20210299229A1 · Yu et al. · 2021 [cited by applicant]
BR 0820483A2 · 2022 [cited by applicant]
RU 2129609C1 · 1999 [cited by applicant]
RU 2277345C1 · 2006 [cited by applicant]
RU 2529949C2 · 2014 [cited by applicant]
WO 8402921A2 · 1984 [cited by applicant]
WO 9200381A1 · 1992 [cited by applicant]
WO 0004136A1 · 2000 [cited by applicant]
WO 2003068256A1 · 2003 [cited by applicant]
WO 2005052148A2 · 2005 [cited by applicant]
WO 2005123911A2 · 2005 [cited by applicant]
WO 200806881A1 · 2008 [cited by applicant]
WO 2013110766A1 · 2013 [cited by applicant]
WO 2013169645A1 · 2013 [cited by applicant]
WO WO2014020142A1 · 2014 [cited by examiner]
WO 2014099415A1 · 2014 [cited by applicant]
WO 2014099416A1 · 2014 [cited by applicant]
WO 2015128366A2 · 2015 [cited by applicant]
CAZy, “Glycoside Hydrolase Family 15”; Carbohydrate-Active Enzymes Database, https://www.cazy.org/GH15_characterized.html (accessed Jan. 2025)). (Year: 2025). [cited by examiner]
Boel et al., “Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs”, The EMBO Journal, vol. 3, No. 5, 1984, pp. 1097-1102. [cited by applicant]
Chen et al., “Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production of Aspergillus awamori glucoamylase”, Protein Engineering, vol. 9, No. 6, 1996, pp. 499-50… [cited by applicant]
Hata et al., “The Glucoamylase cDNA from Aspergillus oryzae: Its Cloning, Nucleotide Sequence, and Expression in [cited by applicant]
Fagerstrom et al., “Characterization, subsite mapping and partial amino acid sequence of glucoamylase from the filamentous fungus [cited by applicant]
Swanson et al., “Kinetics of Maltose Hydrolysis by Glucoamylase”, Biotechnology and Bioengineering, vol. 19, Issue 11, p. 1715-1718 (Year: 1977). [cited by applicant]
Westreicher-Kristen et al., “Postruminal digestion of starch infused into the abomasum of heifers with or without exogenous amylase administration”, J. Anim. Sci. 2018.96:1939-1951. [cited by applicant]
Robbers, “Postruminal digestion of abomasally infused corn starch with or without exogenous amylase administration in cattle”, Dissertation: Faculaty of Agricultural & Nutritional Sciences the Christian Albrechts Univer… [cited by applicant]
Trotta et al., “Duodenal Infusions of Starch with Casein or Glutamic Acid Influence Pancreatic and Small Intestinal Carbohydrase Activities in Cattle”, The Journal of Nutrition, vol. 150, Issue 4, Apr. 2020, pp. 784-791. [cited by applicant]
Remillard, “Starch digestion and digesta kinetics in the small intestine of steers fed on a maize grain and maize silage mixture”, Animal Feed Science and Technology, vol. 30, Issues 1-2, Jul. 1990, pp. 79-89. [cited by applicant]