Degradation of arabinans by arabinanases from Aspergillus aculeatus and Aspergillus niger

An endo-arabinanase was purified from an enzyme preparation, derived from Aspergillus aculeatus. After SDS-gel electrophoresis a molecular weight of 45 kDa was estimated. The enzyme was reactive with antibodies raised against endo-arabinanase from Aspergillus niger, having the same molecular weight....

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Bibliographic Details
Published in:Carbohydrate polymers 1993, Vol.20 (3), p.159-168
Main Authors: Beldman, G., Searle-van Leeuwen, M.J.F., De Ruiter, G.A., Siliha, H.A., Voragen, A.G.J.
Format: Article
Language:English
Subjects:
antibodies
Applied sciences
arabinofuranosidase b
arabinose
Aspergillus aculeatus
Aspergillus niger
Biological and medical sciences
Biotechnology
endo-arabinasase
enzyme activity
Enzyme engineering
Exact sciences and technology
Food Chemistry and Microbiology
Fundamental and applied biological sciences. Psychology
glycosidases
glycosidic linkages
Improved methods for extraction and purification of enzymes
Levensmiddelenchemie en -microbiologie
Methods. Procedures. Technologies
Natural polymers
Physicochemistry of polymers
purification
stability
Starch and polysaccharides
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Summary:An endo-arabinanase was purified from an enzyme preparation, derived from Aspergillus aculeatus. After SDS-gel electrophoresis a molecular weight of 45 kDa was estimated. The enzyme was reactive with antibodies raised against endo-arabinanase from Aspergillus niger, having the same molecular weight. Besides similarities, remarkable differences were observed for endo-arabinanases from A. niger and A. aculeatus. The enzyme from A. aculeatus was optimally active at a higher pH and produced a different spectrum of oligomers after incubation with linear arabinan. This was reflected in a relatively low concentration of oligomers with a degree of polymerization (DP) of 13 and a high concentration of oligomers with a DP of 6–7. Contrary to this, the concentration of oligomers produced by the A. niger endo-arabinanase gradually increased, going from DP 20 to DP 3. Both endo-arabinanases, as well as arabinofuranosidase B from A. niger, were studied with respect to the degradation of branched arabinans. Removal of arabinofuranosyl side chains by arabinofuranosidase B was essentially independent of the type of glycosidic linkage but had a tremendous effect on the digestibility by endo-arabinanase.
ISSN:0144-8617
1879-1344
DOI:10.1016/0144-8617(93)90146-U