期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 71, 期 3-4, 页码 85-89出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2011.04.002
关键词
Lipase; Immobilization; Cross-linked enzyme aggregates; Esterification; Surfactant
资金
- TUBITAK (The Scientific and Technological Research Council of Turkey)
- Research Foundation of Ege University [Sci 2007-011]
Cross-linked enzyme aggregates (CLEA (R) s) were prepared from Candida rugosa lipase (CrL) using glutaraldehyde as the cross-linker. The optimum conditions of the immobilization process were determined (precipitant: ethanol, crosslinker concentration: 25 mM, enzyme concentration: 50 mg/ml, crosslinking time: 45 min.). CLEAs were shown to have several advantages compared to the free enzyme. They were more stable at 50 degrees C and 60 degrees C and had good reusability; retaining 40% of their initial activity after 15 recycles in aqueous media and remaining constant at that level thereafter, suggesting some initial leaching in water. The CLEAs catalyzed esterification reactions in cyclohexane, affording higher conversions than with the free enzyme, especially when longer fatty acids and alcohols were used as substrates. (C) 2011 Elsevier B.V. All rights reserved.
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