Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/65914
Type: Artigo de periódico
Title: Evaluation of Snake Venom Phospholipase A(2): Hydrolysis of Non-Natural Esters
Author: Pirolla, RAS
Baldasso, PA
Marangoni, S
Moran, PJS
Rodrigues, JAR
Abstract: Phospholipase A(2) from the rattlesnake Crotalus durissus terrificus was employed for the first time to test its enantioseletivity on the hydrolysis of different non-natural esters. It was observed that the structure of this small enzyme is restrictive in the choice of its lipase action with non-natural substrates. Two forms of the enzyme were used; free and as its cross-linked enzyme aggregate (CLEA). With all substrates, the free enzyme showed activity similar to the CLEA preparation. The advantage of the CLEA phospholipase is the possibility to reuse it in several consecutive reactions without a decrease of activity and selectivity with good but higher yields and ee than with the free enzyme.
Subject: phospholipase A(2)
snake venom PLA(2)
cross-linking enzyme aggregate
biocatalysis
Country: Brasil
Editor: Soc Brasileira Quimica
Rights: aberto
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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