Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/350532
Type: Artigo
Title: Evaluation of partial purification and immobilization of lipase from geotrichum candidum
Author: Maldonado, Rafael Resende
Aguiar-Oliveira, Elizama
Fogaça, Felipe Massiero
Ramos, Gabriela Giolo
Macedo, Gabriela Alves
Rodrigues, Maria Isabel
Abstract: Partial purification of lipase from Geotrichum candidum was obtained by precipitation using two methods: ethanol (70% v/v) and ammonium sulphate (80% w/v) followed by lyophylization. Recovery factors (RF) from 60% to 140%, concentration factors (CF) from 44 to 66 and lipase activities from 400 to 900 U g−1 were obtained. Lyophylization is important to maintain the enzymatic activity. In relation to solvent affinity, lyophilized lipase had higher affinity for the polar phase when incubated in phosphate buffer:hexane (1:1) but it had lower stability when incubated in phosphate buffer:ethanol (1:1) at 37 °C. Immobilization onto different supports (alginate beads, niobium–graphite alloy, zeolite and Celite®) revealed the inability of niobium–graphite alloy as a support and good potential for the other supports. Under the circumstances applied, Celite® resulted in an immobilized lipase activity around 90 U g−1 and zeolite presented efficiency around 66%, which indicate to be good alternatives for immobilization of lipase from G.candidum
Subject: Lipase
Hidrólise
Country: Países Baixos
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.bcab.2015.05.005
Address: https://www.sciencedirect.com/science/article/pii/S1878818115000717
Date Issue: 2015
Appears in Collections:FEA - Artigos e Outros Documentos
COTUCA - Artigos e Outros Documentos

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