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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
; ; ; ; ; and
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
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004), Biochemistry and Structural Biology (S) (000006142)
id
95ac2ffb-40df-49aa-b126-725356fd3427 (old id 42301)
date added to LUP
2016-04-01 12:24:25
date last changed
2022-01-27 03:16:29
@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}},
  keywords     = {{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}},
  doi          = {{10.1016/S0168-1656(99)00172-8}},
  volume       = {{75}},
  year         = {{1999}},
}