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Sociedade Brasileira de Química, SBQ, Journal of the Brazilian Chemical Society, 4(22), p. 807-807, 2011

DOI: 10.1590/s0103-50532011000400027

Sociedade Brasileira de Química, SBQ, Journal of the Brazilian Chemical Society, 2(22), p. 300-307, 2011

DOI: 10.1590/s0103-50532011000200016

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Evaluation of snake venom phospholipase A2: hydrolysis of non-natural esters

Journal article published in 2011 by Pirolla,Renan A. S., Moran,Paulo J. S., Renan A. S. Pirolla ORCID, Baldasso,Paulo A., Paulo A. Baldasso, Sérgio Marangoni, Marangoni,Sérgio, Paulo J. S. Moran, Rodrigues,José Augusto R., José Augusto R. Rodrigues
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.