Synthesis of geranyl acetate by lipase entrap‐immobilized in cellulose acetate‐TiO 2 gel fiber
Abstract Lipase from Candida antarctica was entrap‐immobilized in cellulose acetate‐TiO 2 gel fiber (fiber‐immobilized lipase) by the sol‐gel method. Syntheses of geranyl acetate and citronellyl acetate catalyzed by the fiber‐immobilized lipase were studied in heptane solution. Conversions reached 8...
| Published in: | Journal of the American Oil Chemists' Society |
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| Main Authors: | , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2001
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1007/s11746-001-0396-7 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1007%2Fs11746-001-0396-7 https://onlinelibrary.wiley.com/doi/full/10.1007/s11746-001-0396-7 |
| Summary: | Abstract Lipase from Candida antarctica was entrap‐immobilized in cellulose acetate‐TiO 2 gel fiber (fiber‐immobilized lipase) by the sol‐gel method. Syntheses of geranyl acetate and citronellyl acetate catalyzed by the fiber‐immobilized lipase were studied in heptane solution. Conversions reached 85% for geranyl acetate after 100 h, and 75% for citronellyl acetate after 80 h, and these values were almost identical to those for syntheses catalyzed by nonimmobilized lipase, although the reaction rate was decreased by immobilization. Compared to those of the non‐immobilized lipase and commercially available immobilized lipase (Novozyme 435), the activity of the fiber‐immobilized lipase was not particularly affected by changes in reaction conditions, such as bulk water content or substrate concentration. The fiber‐immobilized lipase retained a high level of activity after six repeated uses, and almost no enzyme leakage from fiber was observed. However, the reactivity of the fiber‐immobilized lipase was depressed at higher temperature, presumably due to dehydration by thermal contraction of the gel fiber. |
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