Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/337428
Type: Artigo
Title: Thermotolerant lipase from Penicillium sp. section Gracilenta CBMAI 1583: Effect of carbon sources on enzyme production, biochemical properties of crude and purified enzyme and substrate specificity
Author: Turati, Daniela Flavia M.
Almeida, Alex F.
Terrone, Carol C.
Nascimento, Juliana M. F.
Terrasan, Cesar R. F.
Fernandez-Lorente, Gloria
Pessela, Benevides C.
Guisan, Jose M.
Carmona, Eleonora C.
Abstract: In this study, Penicillium sp. section Gracilenta CBMAI 1583 was used to produce lipase under submerged conditions. The enzyme was purified and the biochemical properties of both the crude and purified enzymes were evaluated. Maximum lipase production (1.62 U mL(-1)) was obtained using olive oil 0.5% (w v(-1)) after 72 h of cultivation, representing a 90% increase in the lipase initially produced. The enzyme was purified using hydrophobic interaction chromatography (phenyl Sepharose) under conditions which allowed its interfacial activation. The partially purified sample showed an enzyme with esterase activity (65.4 kDa) on alpha- and beta-naphthyl acetate and other with lipase activity (52.9 kDa) on octyl oleate. Optimum activity of crude and purified lipase was observed at pH 4.0 and 70 degrees C. The purified lipase was activated by NaCl, BaCl2, NH4Cl, MnSO4 and MgSO4; it also presented high stability in organic solvents such as hexane, 2.2.4-trimethylpentane, acetone, DMSO and toluene. Maximum enzyme activity was observed with p-nitrophenyl decanoate as substrate; and the enzyme kinetics showed to be directly affected by Triton X-100. The enzyme shows potential application in processes that operate in acid pH, such as treatment of dairy and industry effluents, resolution of esters in the pharmaceutical industry or in the food industry, as well in synthesis reaction under non-aqueous conditions
Subject: Penicilina
Lipase
Country: Países Baixos
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.bcab.2018.10.002
Address: https://www.sciencedirect.com/science/article/pii/S1878818118303207
Date Issue: 2019
Appears in Collections:IB - Artigos e Outros Documentos

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