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Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05

Paper ID Volume ID Publish Year Pages File Format Full-Text
17765 42694 2009 7 PDF Available
Title
Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05
Abstract

A halostable cellulase with a molecular mass of 29 kDa was purified from culture supernatants of the halophilic bacterium Salinivibrio sp. NTU-05 by way of the Fast Protein Liquid Chromatography method and the biochemical properties of the halostable cellulase was studied. The enzyme was active over a range of 0–25% sodium chloride examined in culture broth. The optimum cellulase activity was observed at 5% sodium chloride. Results from the salinity stability test indicated 24% of enzyme activity was retained at 25% sodium chloride for 4 h. The enzyme was also shown to be slightly thermostable with 40% residual activity under 60 °C for 4 h. The enzyme has a Km of 3.03 mg/ml and a Vmax of 142.86 mol/min/mg when tested using carboxymethyl-cellulose (CMC). The enzyme activity increased in the presence of K+, Mg2+, Na+ ions and decreased when Hg2+ ions were present. The deduced internal amino acid sequence of the Salinivibrio sp. NTU-05 cellulase showed similarity to the sequence of the glycoside hydrolase family protein. These are some of the novel characteristics that make this enzyme have potential applications in cellulose biodegradation.

Keywords
Carboxymethyl-cellulose; Cellulase; Salinivibrio sp.; Halo-tolerant; Purified
First Page Preview
Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 44, Issues 6–7, 8 June 2009, Pages 373–379
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering