Literature DB >> 8520117

Purification and properties of endo-beta-1,4-D-galactanase from Aspergillus niger.

F Yamaguchi1, S Inoue, C Hatanaka.   

Abstract

An endo-beta-1,4-D-galactanase was purified 1735-fold from a commercial enzyme preparation of Aspergillus niger. The endogalactanase was homogeneous by SDS-PAGE, having an apparent molecular weight of 32,000. It specifically hydrolyzed beta-1,4-D-galactan, and is shown to be capable of releasing galactosyl oligomers and galactose from the soybean pectic polysaccharides.

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Year:  1995        PMID: 8520117     DOI: 10.1271/bbb.59.1742

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  3 in total

1.  Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases.

Authors:  Stephanie Shipkowski; Jean E Brenchley
Journal:  Appl Environ Microbiol       Date:  2006-10-20       Impact factor: 4.792

Review 2.  Aspergillus enzymes involved in degradation of plant cell wall polysaccharides.

Authors:  R P de Vries; J Visser
Journal:  Microbiol Mol Biol Rev       Date:  2001-12       Impact factor: 11.056

3.  Mapping the polysaccharide degradation potential of Aspergillus niger.

Authors:  Mikael R Andersen; Malene Giese; Ronald P de Vries; Jens Nielsen
Journal:  BMC Genomics       Date:  2012-07-16       Impact factor: 3.969

  3 in total

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