Immobilization of Candida rugosa lipase on electrospun cellulose nanofiber membrane |
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| Institution: | 1. Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455760, Fortaleza, CE, Brazil;2. Grupo de Química de Materiais Avançados (GQMat), Universidade Federal do Ceará, Campus do Pici, CP 12100, CEP 60451-970, Fortaleza, CE, Brazil;3. Instituto Federal de Educação, Ciência e Tecnologia do Rio Grande do Norte, Campus Apodi, CEP 59700-000, Apodi, RN, Brazil;4. Departamento de Química Orgânica e Inorgânica, Universidade Federal do Ceará, Campus do Pici, CEP 60455760, Fortaleza, CE, Brazil;5. Departamento de Física, Universidade Federal do Rio Grande do Norte, CEP 59078900 Natal, RN, Brazil;6. Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, Campus das Auroras, CEP 62790970, Redenção CE, Brazil;1. Department of Environmental Health Engineering, School of Public Health, Zanjan University of Medical Sciences, Zanjan, Iran;2. National Institute of Genetic Engineering and Biotechnology (NIGEB), P.O. Box:14965/161, Tehran, Iran;1. Department of Microbial Engineering, Konkuk University, Seoul 143-701, South Korea;2. Department of Textile Engineering, Konkuk University, Seoul 143-701, South Korea;3. Department of Chemical Engineering, Kwangwoon University, Seoul 139-701, South Korea;4. Department of Advanced Materials & Chemical Engineering, Hannam University, Daejeon 305-811, South Korea;1. Department of Chemistry, University of Isfahan, Isfahan, 81746-73441, Iran;2. Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan, Isfahan 73441-81746, Iran |
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| Abstract: | A biocatalyst with high activity retention of lipase was fabricated by the covalent immobilization of Candida rugosa lipase on a cellulose nanofiber membrane. This nanofiber membrane was composed of nonwoven fibers with 200 nm nominal fiber diameter. It was prepared by electrospinning of cellulose acetate (CA) and then modified with alkaline hydrolysis to convert the nanofiber surface into regenerated cellulose (RC). The nanofiber membrane was further oxidized by NaIO4. Aldehyde groups were simultaneously generated on the nanofiber surface for coupling with lipase. Response surface methodology (RSM) was applied to model and optimize the modification conditions, namely NaIO4 content (2–10 mg/mL), reaction time (2–10 h), reaction temperature (25–35 °C) and reaction pH (5.5–6.5). Well-correlating models were established for the residual activity of the immobilized enzyme (R2 = 0.9228 and 0.8950). We found an enzymatic activity of 29.6 U/g of the biocatalyst was obtained with optimum operational conditions. The immobilized lipase exhibited significantly higher thermal stability and durability than equivalent free enzyme. |
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