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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Published in | Biotechnology letters Vol. 12; no. 11; pp. 811 - 816 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
01.11.1990
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Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0141-5492 |
DOI: | 10.1007/BF01022600 |