Enzymatic synthesis of fatty esters by alkylated lipase

Autor:	Abu Bakar Salleh, K. Ampon, Mahiran Basri, Che Nyonya Abdul Razak, Wan Md Zin Wan Yunus
Rok vydání:	1997
Předmět:	chemistry.chemical_classification biology Process Chemistry and Technology Triacylglycerol lipase Acetaldehyde Chemical modification Bioengineering Alkylation Biochemistry Catalysis Candida rugosa chemistry.chemical_compound Enzyme chemistry biology.protein Organic chemistry Lipase Selectivity
Zdroj:	Journal of Molecular Catalysis B: Enzymatic. 3:171-176
ISSN:	1381-1177
Popis:	Lipase from Candida rugosa was chemically modified by reductive alkylation with aldehydes of various chain lengths. The derivatised lipases showed a higher esterification activity compared to native enzyme. The degree of activity enhancement depended on the type and molecular weight of the modifiers used and the degree of modification of the enzyme. They exhibited higher activities in non-polar than in polar solvents. The optimum esterification temperature and preference of fatty acids as acyl donors of the derivatised lipases were very similar to those of native enzyme. Lipase derivatised with dodecyldehyde was more thermostable than those modified with acetaldehyde. Alkylated lipases are relatively more stable in organic solvents than the native enzyme.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::38058fecf2c1b5cef456eadf66abac51 https://doi.org/10.1016/s1381-1177(96)00054-9 Zobrazit plný text záznamu Full Text from ScienceDirect