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• W2099104176 abstract "From an Aspergillus niger preparation, which was found to be rich in arabinanase activity, three arabinan-degrading enzymes were purified and characterized for chemical and kinetic parameters. Their pattern of action, substrate specificity and synergism on various L-arabinans were studied. Arabinofuranosidase I was found to be only active on low oligomeric arabinosides; arabinofuranosidase II preferentially hydrolysed the side chain L-arabinose residues from L-arabinan, L-arabinoxylan and L-arabinogalactan. Endo-arabinanase showed optimal activity on linear arabinan with progressively decreasing activity as the linear sequences were more substituted. It accumulated arabinobiose and -triose as end products and was found to act synergistically with both arabinosidase I and II. The technological role of arabinanases in the recent arabinan-haze problems in apple and pear juices as a result of modifications in the traditional processes is discussed." @default.
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• W2099104176 date "1987-12-01" @default.
• W2099104176 modified "2023-09-24" @default.
• W2099104176 title "The degradation of arabinans by endo-arabinanase and arabinofuranosidases purified from Aspergillus niger" @default.
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• W2099104176 doi "https://doi.org/10.1016/s0268-005x(87)80036-x" @default.
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