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Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase

Ademark, Pia; Varga, Arthur LU ; Medve, József; Harjunpää, Vesa; Drakenberg, Torbjörn LU ; Tjerneld, Folke LU and Stålbrand, Henrik LU (1998) In Journal of Biotechnology 63(3). p.199-210
Abstract
The enzymes needed for galactomannan hydrolysis, i.e. β-mannanase, α-galactosidase and β-mannosidase, were produced by the filamentous fungus Aspergillus niger. The β-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the β-mannanase. Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger β-mannanase was sequenced by Edman degradation, and comparison with... (More)
The enzymes needed for galactomannan hydrolysis, i.e. β-mannanase, α-galactosidase and β-mannosidase, were produced by the filamentous fungus Aspergillus niger. The β-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the β-mannanase. Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger β-mannanase was sequenced by Edman degradation, and comparison with Aspergillus aculeatus β-mannanase indicated high identity. The enzyme most probably lacks a cellulose binding domain since it was unable to adsorb on cellulose. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Hemicellulase, α-Galactosidase, Aspergillus niger, β-Mannanase
in
Journal of Biotechnology
volume
63
issue
3
pages
199 - 210
publisher
Elsevier
external identifiers
  • scopus:0345389971
ISSN
1873-4863
DOI
10.1016/S0168-1656(98)00086-8
language
English
LU publication?
yes
id
2fcd7179-8bb2-4398-bc3a-15533111a0c6 (old id 125459)
date added to LUP
2007-06-26 08:53:04
date last changed
2017-07-09 03:37:06
@article{2fcd7179-8bb2-4398-bc3a-15533111a0c6,
  abstract     = {The enzymes needed for galactomannan hydrolysis, i.e. β-mannanase, α-galactosidase and β-mannosidase, were produced by the filamentous fungus Aspergillus niger. The β-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the β-mannanase. Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger β-mannanase was sequenced by Edman degradation, and comparison with Aspergillus aculeatus β-mannanase indicated high identity. The enzyme most probably lacks a cellulose binding domain since it was unable to adsorb on cellulose.},
  author       = {Ademark, Pia and Varga, Arthur and Medve, József and Harjunpää, Vesa and Drakenberg, Torbjörn and Tjerneld, Folke and Stålbrand, Henrik},
  issn         = {1873-4863},
  keyword      = {Hemicellulase,α-Galactosidase,Aspergillus niger,β-Mannanase},
  language     = {eng},
  number       = {3},
  pages        = {199--210},
  publisher    = {Elsevier},
  series       = {Journal of Biotechnology},
  title        = {Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase},
  url          = {http://dx.doi.org/10.1016/S0168-1656(98)00086-8},
  volume       = {63},
  year         = {1998},
}