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- W2362504491 abstract "Dynamics and mode of acting on xylan of three parts of xylanases (Part A, Part B and Part C) separated and purified from a culture filtrate of Penicillium corylophilum No. P 3 31 were investigated. The K m and V max of the three purified enzymes with birchwood xylan as a substrate were 1.00 mg/mL and 0.159 U/mL for Part A ( pH 4.0, 50 ℃) , 1.59 mg/mL and 0.274 U/mL for Part B (pH 4.0,50 ℃) and 0.85 mg/mL and 0.200 U/mL for Part C (pH 5.5,50 ℃). Based on the dynamic studies, it was deduced that three purified enzymes had the same mode of action on xylan. Xylotriose and xylobiose were main hydrolysates of long chain xylan by these enzymes. Xylooligosaccharides upwards from xylotetraose were immediately hydrolyzed, and xylotetraose was mainly hydrolyzed to xylobiose. Xylotriose was slowly hydrolyzed, but xylobiose was unable to be further hydrolyzed by these enzymes. The studies on the hydrolysis dynamics of xylan from corncob with crude enzyme showed that the hydrolysis of arabinose side chain was almost simultaneous with the hydrolysis of xylan, therefore it could be concluded that there existed a α L arabinofuranosidase in crude enzyme." @default.
- W2362504491 created "2016-06-24" @default.
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- W2362504491 date "2001-01-01" @default.
- W2362504491 modified "2023-09-23" @default.
- W2362504491 title "Dynamics and Modes of Action of Xylanases from Penicillium corylophilum on Xylan" @default.
- W2362504491 hasPublicationYear "2001" @default.
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