| Literature DB >> 1366804 |
C J Gray1, J S Narang, S A Barker.
Abstract
Lipase (EC 3.1.1.3) from Candida cylindraceae has been immobilized by the cellulose-titanium chloride method, and on EP-400 polyethylene, with and without glutaraldehyde crosslinking, to give active preparations when assessed by their ability to catalyse the hydrolysis of tributyrin. In both cases, the use of glutaraldehyde crosslinking was shown to improve the stability of the preparations for repeated use. The lipase immobilized on EP-400 polyethylene was found to be effective in transesterification using tributyrin or triacetin as acyl donors with l-menthol as acceptor. The production of methyl butanoate and of methyl acetate using this immobilized preparation was in each case enhanced in the presence of Amberlite IR 47 Anion exchange resin (OH form).Entities:
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Year: 1990 PMID: 1366804 DOI: 10.1016/0141-0229(90)90155-j
Source DB: PubMed Journal: Enzyme Microb Technol ISSN: 0141-0229 Impact factor: 3.493