Enhancement of pH-stability of a low molecular mass endoglucanase from Fusarium oxysporum by protein pegylation

Christakopoulos, P; Kourentzi, E; Hatzinikolaou, DG; Claeyssens, M; Kekos, D; Macris, BJ

dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kourentzi, E	en
dc.contributor.author	Hatzinikolaou, DG	en
dc.contributor.author	Claeyssens, M	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, BJ	en
dc.date.accessioned	2014-03-01T01:13:43Z
dc.date.available	2014-03-01T01:13:43Z
dc.date.issued	1998	en
dc.identifier.issn	0008-6215	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12686
dc.subject	Chemical modification	en
dc.subject	Endoglucanase	en
dc.subject	pH-Stability	en
dc.subject	Polyethylene glycol	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Chemistry, Applied	en
dc.subject.classification	Chemistry, Organic	en
dc.subject.other	glucan synthase	en
dc.subject.other	macrogol	en
dc.subject.other	article	en
dc.subject.other	chemical modification	en
dc.subject.other	enzyme modification	en
dc.subject.other	enzyme stability	en
dc.subject.other	fusarium oxysporum	en
dc.subject.other	molecular weight	en
dc.subject.other	nonhuman	en
dc.subject.other	pH	en
dc.subject.other	priority journal	en
dc.subject.other	Fusarium oxysporum	en
dc.title	Enhancement of pH-stability of a low molecular mass endoglucanase from Fusarium oxysporum by protein pegylation	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/S0008-6215(98)00284-5	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S0008-6215(98)00284-5	en
heal.language	English	en
heal.publicationDate	1998	en
heal.abstract	The stability of the low molecular mass endoglucanase (23.2 kDa) from Fusarium oxysporum at alkaline pH was enhanced by chemical modification. Two distinct types of amino acid-specific modifiers were used. The first, either cyanuric chloride activated polyethylene glycol (CC-PEG) or polyethylene glycol succinimidyl succinate active ester (SS-PEG), react (more or less specifically) with protein amino groups. The second type, maleimide polyethylene glycol (Mal-PEG), is specific for cysteinyl residues. The enzyme lost almost all of its activity when modified with CC-PEG, whereas no inactivation was observed with SS-PEG and Mal-PEG. The modified endoglucanase showed remarkably enhanced alkaline pH stability. When acting upon cello-oligosaccharides and 4-methylumbelliferyl cello-oligosaccharides, the enzyme preferentially cleaved the internal glycosidic bonds. The modified enzymes mediated a decrease in the viscosity of carboxymethyl cellulose (CMC) associated with the release of only small amounts of reducing sugar. Thus, the modified enzyme retains the endo character of the native enzyme. (C) 1998 Elsevier Science Ltd. All rights reserved.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	Carbohydrate Research	en
dc.identifier.doi	10.1016/S0008-6215(98)00284-5	en
dc.identifier.isi	ISI:000079713600009	en
dc.identifier.volume	314	en
dc.identifier.issue	1-2	en
dc.identifier.spage	95	en
dc.identifier.epage	99	en