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

Author

Summary, in English

Two variants of an endo-β-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 39&#;216 and 39&#;265 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 50-55oC. Their stability decreases rapidly when going from 40 to 50oC. 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

Publishing year

2002

Language

English

Pages

267-277

Publication/Series

Journal of Biotechnology

Volume

92

Issue

3

Document type

Journal article

Publisher

Elsevier

Topic

  • Biological Sciences

Keywords

  • Mytilus edulis
  • Blue mussel
  • Purification
  • β-Mannanase

Status

Published

ISBN/ISSN/Other

  • ISSN: 1873-4863