Transesterification activity of lipases immobilized in a phyllosilicate sol-gel matrix**
Autor: | Thomas A. Foglia, An-Fei Hsu, William N. Marmer, Kerby C. Jones |
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Rok vydání: | 2004 |
Předmět: |
Spiroplasma
Triacylglycerol lipase Bioengineering Burkholderia cepacia Molecular sieve Applied Microbiology and Biotechnology Catalysis Phase Transition Fats chemistry.chemical_compound Organic chemistry Lipase Alkyl chemistry.chemical_classification Degree of unsaturation Esterification Ethanol biology Triglyceride Silicates Membranes Artificial General Medicine Transesterification Enzymes Immobilized Enzyme Activation chemistry biology.protein Oils Biotechnology |
Zdroj: | Biotechnology Letters. 26:917-921 |
ISSN: | 0141-5492 |
DOI: | 10.1023/b:bile.0000025903.11697.ae |
Popis: | Lipases from Pseudomonas cepacia (P.c.) and Thermomyces lanuginosa (T.l.) were immobilized in a phyllosilicate sol-gel matrix and studied for their ability to catalyze the alcoholysis of fats and oils to simple alkyl esters. At 50 degrees C and 48 h reaction immobilized T.l. lipase gave higher alkyl ester yields (70 to 100%) from fats and oils regardless of chain length or degree of unsaturation of the acyl groups in the triacylglycerols than did immobilized P.c. lipase (20-90%), which preferred unsaturated oils. Both immobilized lipases catalyzed ester formation (80-90%) from greases containing a range of free fatty acids (2.6 to 36%). Molecular sieves had no effect on ester yields in the immobilized T.l. lipase-catalyzed alcoholysis of greases but did improve yields (5-10%) in the immobilized P.c. lipase-catalyzed reactions. |
Databáze: | OpenAIRE |
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