Cellobiohydrolase I enzymes

US8637293B2 · kind B2 · utility

Assignee

• Alliance for Sustainable Energy, LLC · US

Inventors

• William S. Adney · Golden, US
• Michael E. Himmel · Littleton, US
• Stephen R. Decker · Berthoud, US
• Eric P. Knoshaug · Golden, US
• Mark R. Nimlos · Golden, US
• Michael F. Crowley · Lakewood, US
• Tina Jeoh · Davis, US

Key dates

• Filing date: May 19, 2008
• Grant date: Jan 28, 2014
• Expiry date: May 19, 2028

Classification

• Technology area (CPC C): Chemistry; Metallurgy
• CPC primary: C12Y302/01091
• WIPO field: Biotechnology
• WIPO sector: Chemistry

Abstract

Provided herein is an isolated Cel7A polypeptide comprising mutations in the catalytic domain of the polypeptide relative to the catalytic domain of a wild type Cel7A polypeptide, wherein the mutations reduce N-linked glycosylation of the isolated polypeptide relative to the wild type polypeptide. Also provided herein is an isolated Cel7A polypeptide comprising increased O-linked glycosylation of the linker domain relative to a linker domain of a wild type Cel7A polypeptide. The increased O-linked glycosylation is a result of the addition of and/or substitution of one or more serine and/or threonine residues to the linker domain relative to the linker domain of the wild type polypeptide. In some embodiments, the isolated Cel7A polypeptide comprising mutations in the catalytic domain of the polypeptide relative to the catalytic domain of a wild type Cel7A polypeptide further comprises increased O-linked glycosylation of the linker domain relative to a linker domain of a wild type Cel7A polypeptide. The mutations in the catalytic domain reduce N-linked glycosylation of the isolated polypeptide relative to the wild type polypeptide. The addition of and/or substitution of one or more s…