Carboxymethyl xylan-a specific substrate directly differentiating backbone-hydrolysing and side chain-reacting Beta-D-(1-- 4)-xylanases of the mushroom Termitomyces clypeatus
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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| Title |
Carboxymethyl xylan-a specific substrate directly differentiating backbone-hydrolysing and side chain-reacting Beta-D-(1-- 4)-xylanases of the mushroom Termitomyces clypeatus
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| Creator |
Khowala, Suman
Mukherjee, Mina Sengupta, Subhabrata |
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| Subject |
Drug Development/Diagnostics & Biotechnology
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| Description |
The mushroom Termitomyces clypeatus produces two endoxylanases (D) and (X) when grown in media
containing dextrin and xylan as carbon sources, respectively. Endoxylanase (D) showed wide variation
in its activity on different lots of xylan preparations, and its activity was found to be dependent upon
the composition of xylans. The xylose-liberating endoxylanase (X) did not discriminate between different
xylans. The activity of xylanase (D) was found to decrease as the proportion of xylose in different
xylan preparations increased. The dialyzable oligosaccharides from the digestion of xylan by enzyme
(D) contained constituent sugars of xylan, whereas xylose was the main constituent sugar of the
undialyzable fraction. Enzyme (D) also could not liberate any reducing group from carboxymethyl
xylan (CMX), a suitable substrate for viscometric and colorimetric assays of endolytic activity of
xylanases. CMX was found to be modified preferentially at the substituent sugars of xylan rather than
at backbone residues. Thus CMX proved to be a specific substrate for colorimetric assay of true
endoxylanase activity.
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| Date |
1988
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/1448/1/ENZYME_AND_MICROBIAL_TECHNOLOGY__Volume_10___Issue_9___Pages_563%2D567_%2C1988[28].pdf
Khowala, Suman and Mukherjee, Mina and Sengupta, Subhabrata (1988) Carboxymethyl xylan-a specific substrate directly differentiating backbone-hydrolysing and side chain-reacting Beta-D-(1-- 4)-xylanases of the mushroom Termitomyces clypeatus. Enzyme and Microbial Technology, 10 (9). pp. 563-567. |
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| Relation |
http://dx.doi.org/10.1016/0141-0229(88)90051-8
http://www.eprints.iicb.res.in/1448/ |
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