Work

CelAB, a Multifunctional Cellulase Encoded by Teredinibacter turnerae T7902 T , a Culturable Symbiont Isolated from the Wood-Boring Marine Bivalve Lyrodus pedicellatus

Year: 2007

Type: article

Abstract: We characterized a multifunctional cellulase (CelAB) encoded by the endosymbiont Teredinibacter turnerae T7902(T). CelAB contains two catalytic and two carbohydrate-binding domains, each separated by polyserine linker regions. CelAB binds cellulose and chitin, degrades multiple complex polysaccharides, and displays two catalytic activities, cellobiohydrolase (EC 3.2.1.91) and beta-1,4(3) endoglucanase (EC 3.2.1.4).

Source: Applied and Environmental Microbiology

DOI: 10.1128/aem.00876-07

Authors: Nathan A. Ekborg, Wendy Morrill, Adam M. Burgoyne, Li Li, Daniel L. Distel

Institution: University of Maine

Language: English

Topic: Enzyme Production and Characterization

Subfield: Biotechnology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Science Foundation

Award: Collaborative Research: Functional and genomic analysis of polysymbiosis in the wood-boring bivalve Lyrodus pedicellatus