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KMID : 0379119960240040255
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Korean Journal of Mycology
1996 Volume.24 No. 4 p.255 ~ p.264
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Mode of Action and Chemical Modification of an Alkaline Xyanase (CX-3) from Alkalophilic Cephalosporium sp. RYM-202
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Abstract
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The hydrolysis products formed from birchwood xylan by the action of an aikaline xylanase (CX-III) from alkalophilic Cephadosporium sp. RYM-202 were xylobiose and xylooligosaccharides polymerized with more than 4 sugar molecules. This enzyme was not active on xylobiose but readily attacked xylotriose accumulating xylobiose as a major product. The predominant end-products from xylotetraose by CX-III were xylobiose and xylotriose. These results indicate that the enzyme is typically endo-type xylanase possessing transglyeosidase activity. chemical modification of CX-III with N-bromosuccinimide revealed that two tryptophan residues per molecule of CX-III were essential for its catalytic activity on xylan. On the other hand, iodoacetamide and diethylpyrocarbonate did not influence the activity of the enzyme, suggesting that cysteine and histidine residues are not involved in the active site of this alkaline xylanase.
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