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Characterization of a Neocallimastix patriciarum xylanase gene and its product.

Authors
Type
Published Article
Journal
Canadian Journal of Microbiology
0008-4166
Publisher
Canadian Science Publishing
Publication Date
Volume
45
Issue
11
Pages
970–974
Identifiers
PMID: 10588045
Source
Medline

Abstract

A xylanase gene (xynC) isolated from the anaerobic ruminal fungus Neocallimastix patriciarum was characterized. The gene consists of an N-terminal catalytic domain that exhibited homology to family 11 of glycosyl hydrolases, a C-terminal cellulose binding domain (CBD) and a putative dockerin domain in between. Each domain was linked by a short linker domain rich in proline and alanine. Deletion analysis demonstrated that the CBD was essential for optimal xylanase activity of the enzyme, while the putative dockerin domain may not be required for enzyme function.

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