endo-β-1,4-Mannanases from blue mussel, Mytilus edulis: purification, characterization, and mode of action
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/122981
- author
- Xu, B ; Hägglund, Per LU ; Stålbrand, Henrik LU and Janson, J-C
- organization
- publishing date
- 2002
- 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
- 2016-04-01 12:14:48
- date last changed
- 2022-01-27 00:55:18
@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}},
keywords = {{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}},
doi = {{10.1016/S0168-1656(01)00367-4}},
volume = {{92}},
year = {{2002}},
}