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

In English

Författare

Summary, in English

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.

Publiceringsår

1998

Språk

Engelska

Sidor

199-210

Publikation/Tidskrift/Serie

Journal of Biotechnology

Volym

63

Issue

3

Dokumenttyp

Artikel i tidskrift

Förlag

Elsevier

Ämne

  • Biological Sciences

Nyckelord

  • Hemicellulase
  • α-Galactosidase
  • Aspergillus niger
  • β-Mannanase

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1873-4863