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Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger. J. Biotechnol. 75: 281-289.

Ademark, Pia; Lundqvist, Jon LU ; Hägglund, Per LU ; Tenkanen, M; Torto, N; Tjerneld, Folke LU and Stålbrand, Henrik LU (1999) In Journal of Biotechnology 75(2-3). p.281-289
Abstract
A β-mannosidase was purified to homogeneity from the culture filtrate of Aspergillus niger. A specific activity of 500 nkat mg−1 and a 53-fold purification was achieved using ammonium sulfate precipitation, anion-exchange chromatography, and gel filtration. The isolated enzyme has an isoelectric point of 5.0 and appears to be a dimer composed of two 135-kDa subunits. It is a glycoprotein and contains 17% N-linked carbohydrate by weight. Maximal activity was observed at pH 2.4–5.0 and at 70°C. The β-mannosidase hydrolyzed β-1,4-linked manno-oligosaccharides of degree of polymerization (DP) 2–6 and also released mannose from polymeric ivory nut mannan and galactomannan. The Km and Vmax values for p-nitrophenyl-β-Image-mannopyranoside were... (More)
A β-mannosidase was purified to homogeneity from the culture filtrate of Aspergillus niger. A specific activity of 500 nkat mg−1 and a 53-fold purification was achieved using ammonium sulfate precipitation, anion-exchange chromatography, and gel filtration. The isolated enzyme has an isoelectric point of 5.0 and appears to be a dimer composed of two 135-kDa subunits. It is a glycoprotein and contains 17% N-linked carbohydrate by weight. Maximal activity was observed at pH 2.4–5.0 and at 70°C. The β-mannosidase hydrolyzed β-1,4-linked manno-oligosaccharides of degree of polymerization (DP) 2–6 and also released mannose from polymeric ivory nut mannan and galactomannan. The Km and Vmax values for p-nitrophenyl-β-Image-mannopyranoside were 0.30 mM and 500 nkat mg−1, respectively. Hydrolysis of Image-galactose substituted manno-oligosaccharides showed that the β-mannosidase was able to cleave up to, but not beyond, a side group. An internal peptide sequence of 15 amino acids was highly similar to that of an Aspergillus aculeatus β-mannosidase belonging to family 2 of glycosyl hydrolases. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Hydrolysis, Manno-oligosaccharides, Aspergillus niger, β-Mannosidase
in
Journal of Biotechnology
volume
75
issue
2-3
pages
281 - 289
publisher
Elsevier
external identifiers
  • scopus:0032845641
ISSN
1873-4863
DOI
10.1016/S0168-1656(99)00172-8
language
English
LU publication?
yes
id
95ac2ffb-40df-49aa-b126-725356fd3427 (old id 42301)
date added to LUP
2007-07-17 14:30:33
date last changed
2017-01-22 03:35:19
@article{95ac2ffb-40df-49aa-b126-725356fd3427,
  abstract     = {A β-mannosidase was purified to homogeneity from the culture filtrate of Aspergillus niger. A specific activity of 500 nkat mg−1 and a 53-fold purification was achieved using ammonium sulfate precipitation, anion-exchange chromatography, and gel filtration. The isolated enzyme has an isoelectric point of 5.0 and appears to be a dimer composed of two 135-kDa subunits. It is a glycoprotein and contains 17% N-linked carbohydrate by weight. Maximal activity was observed at pH 2.4–5.0 and at 70°C. The β-mannosidase hydrolyzed β-1,4-linked manno-oligosaccharides of degree of polymerization (DP) 2–6 and also released mannose from polymeric ivory nut mannan and galactomannan. The Km and Vmax values for p-nitrophenyl-β-Image-mannopyranoside were 0.30 mM and 500 nkat mg−1, respectively. Hydrolysis of Image-galactose substituted manno-oligosaccharides showed that the β-mannosidase was able to cleave up to, but not beyond, a side group. An internal peptide sequence of 15 amino acids was highly similar to that of an Aspergillus aculeatus β-mannosidase belonging to family 2 of glycosyl hydrolases.},
  author       = {Ademark, Pia and Lundqvist, Jon and Hägglund, Per and Tenkanen, M and Torto, N and Tjerneld, Folke and Stålbrand, Henrik},
  issn         = {1873-4863},
  keyword      = {Hydrolysis,Manno-oligosaccharides,Aspergillus niger,β-Mannosidase},
  language     = {eng},
  number       = {2-3},
  pages        = {281--289},
  publisher    = {Elsevier},
  series       = {Journal of Biotechnology},
  title        = {Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger. J. Biotechnol. 75: 281-289.},
  url          = {http://dx.doi.org/10.1016/S0168-1656(99)00172-8},
  volume       = {75},
  year         = {1999},
}