Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/5125
Title: A unique thermostable lichenase from Thermotoga maritima MSB8 with divergent substrate specificity
Authors: Khan, Mohammed Abdul Sattar
Akbar, Mohammed
Kitaoka, Motomitsu
Hayashi, Kiyoshi
Keywords: Thermotoga maritima;endoglucanase;lichenase;family 5;glucosyl β-1;3 glucosyl β-1;4 glucose;glucosyl β-1;4 glucosyl β-1;3 glucose
Issue Date: Jul-2007
Publisher: CSIR
IPC Code: Int. Cl.8 C12N9/24
Abstract: A putative endoglucanase gene corresponding to locus TM 1752 (AAD36817.1, Q9X274) of Thermotoga maritima MSB8 was cloned and expressed in Escherichia coli. The enzyme contains a NEP (Asn-Glu-Pro) motif but lacks a PCD (proposed catalytic domain) block. This endoglucanase is grouped under family 5 of the glycosyl hydrolases members of which predominantly hydrolyze β-1,4-linkages of carbohydrate polymers. The enzyme efficiently hydrolyzes the glycosidic bonds of mixed β-1,3-1,4 linkages in lichenan and barley β-glucan, but did not display any activity on crystalline cellulose or laminarin. However, negligible amount of hydrolysis was observed with CM-cellulose. This enzyme produced glucosyl β-1,3 glucosyl β-1,4 glucose as the major end product and glucosyl β-1,4 glucosyl β-1,3 glucose was not detected. The putative endoglucanase of T. maritima appears to be a unique endoglucanase being the first lichenase producing glucosyl β-1,3 glucosyl β-1,4 glucose to be placed into family 5 of the glucosyl hydrolases.
Page(s): 315-320
URI: http://hdl.handle.net/123456789/5125
ISSN: 0975-0967 (Online); 0972-5849 (Print)
Appears in Collections: IJBT Vol.06(3) [July 2007]

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