Characterization and catalytic properties of a new crude lipase from C. rugosa

Autor:	R.M. de la Casa, J.M. Sánchez-Montero, Jose‐Vicente Sinisterra
Rok vydání:	2006
Předmět:	biology Chemistry Triacylglycerol lipase Bioengineering Applied Microbiology and Biotechnology Biochemistry Catalysis Candida rugosa Acylation Hydrolysis Oleic acid chemistry.chemical_compound biology.protein Organic chemistry Organic synthesis Lipase Biotechnology
Zdroj:	Enzyme and Microbial Technology. 38:599-609
ISSN:	0141-0229
DOI:	10.1016/j.enzmictec.2005.05.017
Popis:	Using fed-batch controlled fermenter conditions and oleic acid as the only carbon source, a new crude lipase from Candida rugosa ATCC 14830 (UAB) was produced. This lipase is a mixture of Lip2 (43%) and Lip3 (57%) and shows different composition in isoenzymes than commercial lipase from Sigma, CRL (17% Lip3 and 83% Lip1) and different content in carbohydrates. Both biocatalysts show different catalytic activity in the hydrolysis of triglycerides and in organic synthesis in slightly hydrated organic solvents with a w control: (i) heptyl oleate synthesis, (ii) 2-arylpropionic acids esterification and (iii) acylation of different terpenic alcohols. From the structure–activity scope we show that Lip2 is an isoenzyme, which accepts large molecules – acyl donor or acyl acceptor – and that Lip1 is very active versus unbranched structures but requires water in the microenvironment to be active.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f4d3392f0492699a645290cc3d618d0d https://doi.org/10.1016/j.enzmictec.2005.05.017 Zobrazit plný text záznamu Full Text from ScienceDirect