Affordable Access

endo-beta-1,4-Mannanases from blue mussel, Mytilus edulis: purification, characterization, and mode of action.

Authors
  • Xu, Bingze
  • Hägglund, Per
  • Stålbrand, Henrik
  • Janson, Jan-Christer
Type
Published Article
Journal
Journal of Biotechnology
Publisher
Elsevier
Publication Date
Jan 18, 2002
Volume
92
Issue
3
Pages
267–277
Identifiers
PMID: 11689251
Source
Medline
License
Unknown

Abstract

Two variants of an endo-beta-1,4-mannanase from the digestive tract of blue mussel, Mytilus edulis, were purified by a combination of immobilized metal ion affinity chromatography, size exclusion chromatography in the absence and presence of guanidine hydrochloride and ion exchange chromatography. The purified enzymes were characterized with regard to enzymatic properties, molecular weight, isoelectric point, amino acid composition and N-terminal sequence. They are monomeric proteins with molecular masses of 39216 and 39265 Da, respectively, as measured by MALDI-TOF mass spectrometry. The isoelectric points of both enzymes were estimated to be around 7.8, however slightly different, by isoelectric focusing in polyacrylamide gel. The enzymes are stable from pH 4.0 to 9.0 and have their maximum activities at a pH about 5.2. The optimum temperature of both enzymes is around 50-55 degrees C. Their stability decreases rapidly when going from 40 to 50 degrees C. The N-terminal sequences (12 residues) were identical for the two variants. They can be completely renatured after denaturation in 6 M guanidine hydrochloride. The enzymes readily degrade the galactomannans from locust bean gum and ivory nut mannan but show no cross-specificity for xylan and carboxymethyl cellulose. There is no binding ability observed towards cellulose and mannan.

Report this publication

Statistics

Seen <100 times