Purification and properties of a low molecular weight 1,4-β-d-glucan glucohydrolase having one active site for carboxymethyl cellulose and xylan from an alkalothermophilic Thermomonospora sp.
- 1 April 2005
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 329 (1) , 111-116
- https://doi.org/10.1016/j.bbrc.2005.01.102
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- A monovalent anion affected multi-functional cellulase EGX from the mollusca, Ampullaria crosseanProtein Expression and Purification, 2003
- Microbial Cellulose Utilization: Fundamentals and BiotechnologyMicrobiology and Molecular Biology Reviews, 2002
- Studies on carboxymethyl cellulase produced by an alkalothermophilic actinomyceteBioresource Technology, 2001
- Cellulases and related enzymes in biotechnologyBiotechnology Advances, 2000
- Molecular and biotechnological aspects of xylanasesFEMS Microbiology Reviews, 1999
- Butyrivibriospp. and Other Xylanolytic Microorganisms From the Rumen have Cinnamoyl Esterase ActivityAnaerobe, 1998
- Dockerin-like sequences in cellulases and xylanases from the rumen cellulolytic bacterium Ruminococcus flavefaciensFEMS Microbiology Letters, 1997
- Characterization of a Thermomonospora fusca exocellulaseBiochemistry, 1995
- Cellulases of bacterial originEnzyme and Microbial Technology, 1989
- Growth of Cellulomonas sp. ATCC 21399 on different polysaccharides as sole carbon source Induction of extracellular enzymesApplied Microbiology and Biotechnology, 1988