Cloning the Clostridium thermocellum thermostable laminarinase gene in Escherichia coli ; the properties of the enzyme thus produced

We have cloned a 1.9-kb-long fragment of Clostridium thermocellum DNA which encodes laminarinase (EC 3.2.1.39). The enzyme hydrolyzes the beta -1,3-glucoside bonds in beta -1,3- and in mixed beta -1,3-1,4-polyglucans. The enzymes's optimum pH value is around 8.5, temperature optimum -70 degree...

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Bibliographic Details
Published inBiotechnology letters Vol. 12; no. 11; pp. 811 - 816
Main Authors Zverlov, V V, Velikodvorskaya, G A
Format Journal Article
LanguageEnglish
Published 01.11.1990
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Summary:We have cloned a 1.9-kb-long fragment of Clostridium thermocellum DNA which encodes laminarinase (EC 3.2.1.39). The enzyme hydrolyzes the beta -1,3-glucoside bonds in beta -1,3- and in mixed beta -1,3-1,4-polyglucans. The enzymes's optimum pH value is around 8.5, temperature optimum -70 degree C, PAGE-determined mol. weight similar to 32 kDa.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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ISSN:0141-5492
DOI:10.1007/BF01022600