Improved stability and reactivity of Fusarium solani cutinase in supercritical CO sub(2)
Cutinase from Fusarium solani pisi was immobilized on Accurel EP100 and catalyzed the esterification of hexanoic acid with hexanol in supercritical CO sub(2). The enzyme lost only 10% of its activity over six days. Esterification was maximal with a water activity of a sub(w) = 0.76.
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| Published in | Biotechnology techniques Vol. 11; no. 9; pp. 661 - 665 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
01.09.1997
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| Online Access | Get full text |
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| Summary: | Cutinase from Fusarium solani pisi was immobilized on Accurel EP100 and catalyzed the esterification of hexanoic acid with hexanol in supercritical CO sub(2). The enzyme lost only 10% of its activity over six days. Esterification was maximal with a water activity of a sub(w) = 0.76. |
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| Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-1 |
| ISSN: | 0951-208X |