Physical crosslinking of lipase from Rhizomucor miehei immobilized on octyl agarose via coating with ionic polymers: Avoiding enzyme release from the support |
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| Institution: | 1. Departamento de biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain;2. CONACYT – Centro de Investigación en Alimentación y Desarrollo, A.C. (CIAD) – Centro de Innovación y Desarrollo Agroalimentario de Michoacán, A.C. (CIDAM), Km. 8 Antigua Carretera a Pátzcuaro s/n, C.P. 58341, Morelia, Michoacán, Mexico;1. Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Bloco 709, 60455-760 Fortaleza, CE, Brazil;2. Departamento de Química Analítica e Físico-Química, Centro de Ciências, Universidade Federal do Ceará, Av. Mister Hull s/n, Pici, 60455-760, Fortaleza, CE, CP 12200, Brazil;3. Departamento de Química Orgânica e Inorgânica, Centro de Ciências, Universidade Federal do Ceará, Av. Mister Hull s/n, Pici, 60455-760, Fortaleza, CE, CP 12200 Brazil;4. Departamento de Biocatalisis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain;5. Departamento de Física, Universidade Federal do Rio Grande do Norte, 59078-900 Natal, RN, Brazil;6. Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, 62785000 Acarape, CE, Brazil;1. Biotechnology, Bioprocess, and Biocatalysis Group, Food Science and Technology Institute, Federal University of Rio Grande do Sul, Av. Bento Gonçalves 9500, PO Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil;2. Department of Organic Chemistry, Institute of Chemistry, Federal University of Rio Grande do Sul, Av. Bento Gonçalves 9500, PO Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil;3. Department of Biocatalysis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, ZC 28049, Madrid, Spain;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. Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia;1. ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain;2. Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, Fortaleza, CE CEP 60455-760, Brazil;3. Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia;4. Departamento de Química, Grupo de investigación en productos naturales (GIPRONUT), Universidad del Tolima, Ibagué, Colombia |
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| Abstract: | Lipase from Rhizomucor miehei (RML) was immobilized on octyl-agarose (OC) at different loadings. Using low enzyme loadings (1/7 of the maximum loading), the incubation of the enzyme with polyethylenimine (PEI) increased the resistance to enzyme desorption in the presence of Triton X-100. However, more than 10% of the enzyme activity could be released from the OC-RML-PEI. The same treatment using fully loaded biocatalyst reduced the enzyme desorption to less than 5%. Further treatment with dextran sulfate (DS) of the PEI treaded immobilized enzyme fully avoids the enzyme desorption even in presence of a Triton X-100 concentration higher than that required for the complete enzyme release from OC-RML. This treatment produced a high stabilization of OC-RML in thermal or organic solvent inactivations, reducing the enzyme release under these drastic conditions. Nevertheless, the support could be recovered by incubation under adequate conditions, and reused in several adsorption/desorption cycles. Thus, the strategy permitted to avoid enzyme desorption, very likely by physical intermolecular crosslinking improving enzyme stability, while still maintaining the reversibility of the immobilization. |
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| Keywords: | Interfacial activation Lipase immobilization Hydrophobic supports Enzyme desorption Support reuse Enzyme stabilization |
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