Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger. J. Biotechnol. 75: 281-289.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/42301
- author
- Ademark, Pia ; Lundqvist, Jon LU ; Hägglund, Per LU ; Tenkanen, M ; Torto, N ; Tjerneld, Folke LU and Stålbrand, Henrik LU
- organization
- publishing date
- 1999
- 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}}, }