IP Library › Granted Patent US 12,195,776
Granted Patent B2
US 12,195,776 · App. 17/547,836 · Granted Jan 14, 2025

Cellulolytic enzyme compositions and uses thereof

Inventors: Jeffrey Shasky (Davis, CA); Amanda Fischer (Davis, CA); Suchindra Maiyuran (Gold River, CA)
Assignee: Novozymes, Inc.
C12P19/14C07K14/38C12N9/2437C12N9/2445C12P19/02C12Y302/01004C12Y302/01008C12Y302/01021C12Y302/01037C12Y302/01091C12Y302/01176Y02E50/10Y02P20/52
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Quick Facts
Patent No.
US 12,195,776
App. No.
17/547,836
Granted
Jan 14, 2025
Kind
B2
Abstract

The present invention relates to recombinant filamentous fungal host cells producing cellulolytic enzyme compositions and methods of producing and using the compositions.

Claims (22)

1. An enzyme composition, comprising:

(i) a cellobiohydrolase I (CBHI) having at least 80% sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 2;

(ii) a beta-glucosidase having at least 80%, but less than 100%, sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 6 and comprising a substitution at one or more positions corresponding to positions 100, 283, 456, and 512 of the mature polypeptide of SEQ ID NO: 6, wherein the substitution at position 100 is Asp, the substitution at position 283 is Gly, the substitution at position 456 is Glu, and the substitution at position 512 is Tyr; and

(iii) an endoglucanase.

2. The enzyme composition of claim 1 , wherein the CBHI has at least 85% sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 2.

3. The enzyme composition of claim 1 , wherein the CBHI has at least 90% sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 2.

4. The enzyme composition of claim 1 , wherein the CBHI has at least 95% sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 2.

5. The enzyme composition of claim 1 , wherein the CBHI comprises the amino acid sequence of the mature polypeptide of SEQ ID NO: 2.

6. The enzyme composition of claim 1 , wherein the beta-glucosidase has at least 85%, but less than 100%, sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 6 and comprises a substitution at one or more positions corresponding to positions 100, 283, 456, and 512 of the mature polypeptide of SEQ ID NO: 6, wherein the substitution at position 100 is Asp, the substitution at position 283 is Gly, the substitution at position 456 is Glu, and the substitution at position 512 is Tyr.

7. The enzyme composition of claim 1 , wherein the beta-glucosidase has at least 90%, but less than 100%, sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 6 and comprises a substitution at one or more positions corresponding to positions 100, 283, 456, and 512 of the mature polypeptide of SEQ ID NO: 6, wherein the substitution at position 100 is Asp, the substitution at position 283 is Gly, the substitution at position 456 is Glu, and the substitution at position 512 is Tyr.

8. The enzyme composition of claim 1 , wherein the beta-glucosidase has at least 95%, but less than 100%, sequence identity to the amino acid sequence of the mature polypeptide of SEQ ID NO: 6 and comprises a substitution at one or more positions corresponding to positions 100, 283, 456, and 512 of the mature polypeptide of SEQ ID NO: 6, wherein the substitution at position 100 is Asp, the substitution at position 283 is Gly, the substitution at position 456 is Glu, and the substitution at position 512 is Tyr.

9. The enzyme composition of claim 1 , wherein the beta-glucosidase comprises a substitution at one or more positions of positions 100, 283, 456, and 512 of the mature polypeptide of SEQ ID NO: 6, wherein the substitution at position 100 is Asp, the substitution at position 283 is Gly, the substitution at position 456 is Glu, and the substitution at position 512 is Tyr.

10. The enzyme composition of claim 1 , wherein the endoglucanase is a Trichoderma reesei endoglucanase.

11. The enzyme composition of claim 10 , wherein the endoglucanase is Trichoderma reesei endoglucanase I.

12. The enzyme composition of claim 10 , wherein the endoglucanase is Trichoderma reesei endoglucanase II.

13. The enzyme composition of claim 1 , which further comprises one or more enzymes selected from the group consisting of a cellulase, a GH61 polypeptide having cellulolytic enhancing activity, a hemicellulase, an esterase, an expansin, a laccase, a ligninolytic enzyme, a pectinase, a peroxidase, a protease, and a swollenin.

14. A process for degrading a cellulosic material, comprising: contacting the cellulosic material with the enzyme composition of claim 1 .

15. A process for producing a fermentation product, comprising:

(a) saccharifying a cellulosic material with the enzyme composition of claim 1 ;

(b) fermenting the saccharified cellulosic material with one or more fermenting microorganisms to produce the fermentation product; and

(c) recovering the fermentation product from the fermentation.

16. A process of fermenting a cellulosic material, comprising: fermenting the cellulosic material with one or more fermenting microorganisms, wherein the cellulosic material is saccharified with the enzyme composition of claim 1 .

Continuity (4)
Division 16878267 · May 19, 2020
Continuation 16268922 · Feb 6, 2019
Related Publication 20220098631A1 · Mar 31, 2022
Related Publication 20240376507A9 · Nov 14, 2024
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