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

Xu, B; Hägglund, Per LU ; Stålbrand, Henrik LU and Janson, J-C (2002) In Journal of Biotechnology 92(3). p.267-277
Abstract
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.... (More)
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 (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Mytilus edulis, Blue mussel, Purification, β-Mannanase
in
Journal of Biotechnology
volume
92
issue
3
pages
267 - 277
publisher
Elsevier
external identifiers
  • pmid:11689251
  • wos:000173186900007
  • scopus:0037126853
ISSN
1873-4863
DOI
10.1016/S0168-1656(01)00367-4
language
English
LU publication?
yes
id
b2f5ed42-6b35-462c-96f4-bad950dce677 (old id 122981)
date added to LUP
2007-07-06 16:48:47
date last changed
2017-09-17 05:04:22
@article{b2f5ed42-6b35-462c-96f4-bad950dce677,
  abstract     = {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},
  author       = {Xu, B and Hägglund, Per and Stålbrand, Henrik and Janson, J-C},
  issn         = {1873-4863},
  keyword      = {Mytilus edulis,Blue mussel,Purification,β-Mannanase},
  language     = {eng},
  number       = {3},
  pages        = {267--277},
  publisher    = {Elsevier},
  series       = {Journal of Biotechnology},
  title        = {endo-β-1,4-Mannanases from blue mussel, Mytilus edulis: purification, characterization, and mode of action},
  url          = {http://dx.doi.org/10.1016/S0168-1656(01)00367-4},
  volume       = {92},
  year         = {2002},
}