Alliance for Sustainable Energy, LLC

Midwest Research Institute

John O Baker

Michael E Himmel

William S Adney

Stephen Robert Decker

Yat-Chen Chou

Qi Xu

Gregg Tyler Beckham

Eric E Jarvis

Jeffrey G Linger

Shi-You Ding

Arjun Singh

Kara Podkaminer

Larry Taylor, Ii

Todd B Vinzant

Steven R Thomas

Suzanne Mc Carter

Raphael Nieves

Nucleic acid sequences encoding chimeric polypeptides that exhibit enhanced cellulase activities are disclosed herein. These nucleic acids may be expressed in hosts such as fungi, which in turn may be cultured to produce chimeric polypeptides. Also disclosed are chimeric polypeptides and their use in the degradation of cellulosic materials.

Enhanced processive cellulases

Nucleic acid molecules encoding chimeric cellulase polypeptides that exhibit improved cellulase activities are disclosed herein. The chimeric cellulase polypeptides encoded by these nucleic acids and methods to produce the cellulases are also described, along with methods of using chimeric cellulases for the conversion of cellulose to sugars such as glucose.

Chimeric enzymes with improved cellulase activities

Purified cellobiohydrolase I (glycosyl hydrolase family 7 (Cel7A)) enzymes fromdemonstrate a high level of specific performance in comparison to other Cel7 family member enzymes when formulated with purified EIcd endoglucanase fromand tested on pretreated corn stover. This result is true of the purified native enzyme, as well as recombinantly expressed enzyme, for example, that enzyme expressed in a non-nativehost. In a specific example, the specific performance of the formulation using purified recombinant Cel7A fromexpressed inis increased by more than 200% when compared to a formulation using purified Cel7A from

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Purified cellobiohydrolase I (glycosyl hydrolase family 7 (Cel7A) enzymes fromdemonstrate a high level of specific performance in comparison to other Cel7 family member enzymes when formulated with purified EIcd endoglucanase fromand tested on pretreated corn stover. This result is true of the purified native enzyme, as well as recombinantly expressed enzyme, for example, that enzyme expressed in a non-nativehost. In a specific example, the specific performance of the formulation using purified recombinant Cel7A fromexpressed inis increased by more than 200% when compared to a formulation using purified Cel7A from

The disclosure provides a method for preparing an active exoglucanase in a heterologous host of eukaryotic origin. The method includes mutagenesis to reduce glycosylation of the exoglucanase when expressed in a heterologous host. It is further disclosed a method to produce variant cellobiohydrolase that is stable at high temperature through mutagenesis.

Cellobiohydrolase I gene and improved variants

The gene encoding Acidothermus cellulolyticus E1 endoglucanase is cloned and expressed in Pichia pastoris. A new modified E1 endoglucanase enzyme comprising the catalytic domain of the full size E1 enzyme demonstrates enhanced thermostability and is produced by two methods. The first method of producing the new modified E1 is proteolytic cleavage to remove the cellulose binding domain and linker peptide of the full size E1. The second method of producing the new modified E1 is genetic truncation of the gene encoding the full size E1 so that the catalytic domain is expressed in the expression product.

Method for increasing thermostability in cellulase ennzymes

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Golden, CO, United States of America

John O Baker