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Open AccessArticle

Different Covalent Immobilizations Modulate Lipase Activities of Hypocrea pseudokoningii

Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Av. Bandeirantes, 3900, Ribeirão Preto-SP 14040-901, Brazil
Heterogeneous Biocatalysis Group, CIC Biomagune, Parque Tecnológico de San Sebastián Edificio Empresarial “C”, Paseo Miramón 182, 20009 Donostia-San Sebastián Guipúzcoa, Spain
Departamento de Biotecnología y Microbiología de los Alimentos, Instituto de Ciências de la Alimentación, CIAL-CSIC, Calle Nicolás Cabrera 9, Campus UAM, Cantoblanco, 28049 Madrid, Spain
Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica, CSIC, Campus UAM, Cantoblanco, 28049 Madrid, Spain
Departamento de Bioquímica e Imunologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto-SP 14040-900, Brazil
Author to whom correspondence should be addressed.
Molecules 2017, 22(9), 1448;
Received: 3 August 2017 / Accepted: 29 August 2017 / Published: 4 September 2017
(This article belongs to the Special Issue Lipases and Lipases Modification)
Enzyme immobilization can promote several advantages for their industrial application. In this work, a lipase from Hypocrea pseudokoningii was efficiently linked to four chemical supports: agarose activated with cyanogen bromide (CNBr), glyoxyl-agarose (GX), MANAE-agarose activated with glutaraldehyde (GA) and GA-crosslinked with glutaraldehyde. Results showed a more stable lipase with both the GA-crosslinked and GA derivatives, compared to the control (CNBr), at 50 °C, 60 °C and 70 °C. Moreover, all derivatives were stabilized when incubated with organic solvents at 50%, such as ethanol, methanol, n-propanol and cyclohexane. Furthermore, lipase was highly activated (4-fold) in the presence of cyclohexane. GA-crosslinked and GA derivatives were more stable than the CNBr one in the presence of organic solvents. All derivatives were able to hydrolyze sardine, açaí (Euterpe oleracea), cotton seed and grape seed oils. However, during the hydrolysis of sardine oil, GX derivative showed to be 2.3-fold more selectivity (eicosapentaenoic acid (EPA)/docosahexaenoic acid (DHA) ratio) than the control. Additionally, the types of immobilization interfered with the lipase enantiomeric preference. Unlike the control, the other three derivatives preferably hydrolyzed the R-isomer of 2-hydroxy-4-phenylbutanoic acid ethyl ester and the S-isomer of 1-phenylethanol acetate racemic mixtures. On the other hand, GX and CNBr derivatives preferably hydrolyzed the S-isomer of butyryl-2-phenylacetic acid racemic mixture while the GA and GA-crosslink derivatives preferably hydrolyzed the R-isomer. However, all derivatives, including the control, preferably hydrolyzed the methyl mandelate S-isomer. Moreover, the derivatives could be used for eight consecutive cycles retaining more than 50% of their residual activity. This work shows the importance of immobilization as a tool to increase the lipase stability to temperature and organic solvents, thus enabling the possibility of their application at large scale processes. View Full-Text
Keywords: enzyme immobilization; lipase activity modulation; stability; hydrolysis of oils; Hypocrea pseudokoningii enzyme immobilization; lipase activity modulation; stability; hydrolysis of oils; Hypocrea pseudokoningii
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MDPI and ACS Style

Pereira, M.G.; Velasco-Lozano, S.; Moreno-Perez, S.; Polizeli, A.M.; Heinen, P.R.; Facchini, F.D.A.; Vici, A.C.; Cereia, M.; Pessela, B.C.; Fernandez-Lorente, G.; Guisan, J.M.; Jorge, J.A.; Polizeli, M.D.L.T.M. Different Covalent Immobilizations Modulate Lipase Activities of Hypocrea pseudokoningii. Molecules 2017, 22, 1448.

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