Stabilization of the lipase of Hypocrea pseudokoningii by multipoint covalent immobilization after chemical modification and application of the biocatalyst in oil hydrolysis

Autor: Ana Claudia Vici, Aline M. Polizeli, Fernanda Dell Antonio Facchini, Jose M. Guisan, Maria de Lourdes Teixeira de Moraes Polizeli, Gloria Fernández-Lorente, Benevides C. C. Pessela, João Atílio Jorge, Marita Gimenez Pereira
Přispěvatelé: Fundação de Amparo à Pesquisa do Estado de São Paulo, Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)
Rok vydání: 2015
Předmět:
Zdroj: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Digital.CSIC. Repositorio Institucional del CSIC
instname
ISSN: 1381-1177
DOI: 10.1016/j.molcatb.2015.08.008
Popis: Lipase from Hypocrea pseudokoningii was purified using the support Octyl-Sepharose. This adsorption resulted in a 3-fold increase in activity of the immobilized enzyme. Following, still on this support, the lipase was enriched in surface amino groups (by reaction of carboxy groups with ethylendiamine). After amination, the lipase was desorbed from Octyl-Sepharose, while the 2-fold hyper-activation was maintained. The aminated lipase was also successfully immobilized on Glyoxyl-Agarose. The derivative was 45-fold more stable than was the free enzyme at 50 and 60 °C. The derivative was also stable in 50% of organic solvents such as methanol, ethanol, propanol and cyclohexane. The multipoint immobilization also increased the enzyme stability in relation to the free enzyme in the presence of ethanol, methanol and cyclohexane for up to 72 h. For example, the stabilized derivative was 9-fold more stable than the free enzyme in presence of methanol. The derivatives hydrolyzed fish, cupuaçu (Theobroma grandiflorum), bacuri (Latonia insignis) and murumuru (Astrocaryum murumuru) oils. The multipoint immobilization process increased the hydrolysis of oils up to 15-fold compared with the control, what makes these derivatives attractive for industrial application.
This work was supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP), Conselho de Desenvolvimento Científico e Tecnológico (CNPq process n° 406838/2013-5). This project is also part of the National Institute of Science and Technology of the Bioethanol (n° 574002/2008-1), CNPq—Ciência sem Fronteira (n° 242775/2012-8). JAJ and MLTMP are Research Fellows of CNPq. MGP and ACV are supported by CNPq. FDAF was recipient of a FAPESP Fellowship.
Databáze: OpenAIRE
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