Immobilization of lipase in organic solvent in the presence of fatty acid additives |
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| Affiliation: | 1. State Key Laboratory of Food Science and Technology, National Engineering Research Center for Functional Food, National Engineering Laboratory for Cereal Fermentation Technology, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, School of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, Jiangsu, PR China;2. Food and Dairy Science and Technology Department, Faculty of Environmental Agricultural Science, El-Arish University, 43511 El-Arish, Egypt;3. Department of Food Science, Faculty of Agriculture, Zagazig University, 44511 Zagazig, Egypt;1. Departamento de Ingeniería Química, Universidad Nacional del Sur (UNS), Planta Piloto de Ingeniería, Química - PLAPIQUI (UNS-CONICET), Bahía Blanca 8000, Argentina;2. Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto 14040-901, São Paul, Brazil;3. Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Paraná, Cx. P. 19046 Centro Politécnico, Curitiba 81531-980, Paraná, Brazil;4. Departamento de Química, Universidade Federal do Paraná, Cx. P. 19081 Centro Politécnico, Curitiba 81531-980, Paraná, Brazil;5. Departamento de Química, Universidad Nacional del Sur (UNS), Planta Piloto de Ingeniería, Química - PLAPIQUI (UNS-CONICET), Bahía Blanca 8000, Argentina;1. ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain;2. Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, CEP 60455-760 Fortaleza, CE, Brazil;3. Biotechnology, Bioprocess and Biocatalysis Group, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970 Porto Alegre, RS, Brazil;1. Universidade Federal do Rio de Janeiro, Faculdade de Farmácia, Departamento de Biotecnologia Farmacêutica, Centro de Ciências e Saúde, Bloco B, 1 andar (1 floor), Laboratório Multidisciplinar de Pesquisas em Biotecnologia, CEP 21941902, Rio de Janeiro, Brazil;2. Department of Biocatalysis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain;3. Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760, Fortaleza, CE, Brazil;4. Programa de Pós-Graduação em Bioquímica, Departamento de Bioquímica, Brazil;5. Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia |
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| Abstract: | In this study porcine pancreatic lipase (PPL) was covalently immobilized on cross-linked polyvinyl alcohol (PVA) in organic media in the presence of fatty acid additives in order to improve its immobilized activity. The effects of fatty acid additions to the immobilization media were investigated choosing tributyrin hydrolysis in water and ester synthesis by immobilized PPL in n-hexane. Various fatty acids which are also the substrates of lipases in esterification reactions were used as active site protecting agents during the immobilization process in an organic solvent. The obtained results showed that covalent immobilization carried out in the presence of fatty acids as protective ligands improved the hydrolytic and esterification activity of immobilized enzyme. A remarkable increase in activity of the immobilized PPL was obtained when octanoic acid was used as an additive and the hydrolytic activity was increased from 5.2 to 19.2 μmol min−1 mg−1 as compared to the non-additive immobilization method. With the increase of hydrolytic activity of immobilized lipase in the presence of octanoic acid, in an analogous manner, the rate of esterification for the synthesis of butyl octanoate was also increased from 7.3 to 26.3 μmol min−1 g−1 immobilized protein using controlled thermodynamic water activities with saturated salt solutions. In addition, the immobilized PPL activity was maintained at levels representing 63% of its original activity value after 5 repeated uses. The proposed method could be adopted for a wide variety of other enzymes which have highly soluble substrates in organic solvent such as other lipases and esterases. |
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