Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature,immobilization protocol and inactivation conditions |
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| Institution: | 1. Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain;2. Equipe TEPA, Laboratoire LNTA, INATAA, Université des Frères Mentouri Constantine 1, 25000 Constantine, Algeria;3. Department of Chemical and Petroleum Engineering, Sharif University of Technology, Azadi Avenue, 113658639 Tehran, Iran;4. Research Laboratory of Applied Biochemistry, Bouira University, Sidi Aïch, Bejaia, Algeria;5. Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Bloco 709, CEP 60455-760, Fortaleza, CE, Brazil;1. Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC, Madrid, Spain;2. Food Biotechnology Division, Biotechnology Research Center (CRBt), Algeria;3. Applied Microbiology in Environment Laboratory, Science Department, Ibn Khalboun University, Algeria;4. Transformation and Food Product Elaboration Laboratory, Nutrition and Food Technology Institute (INATAA), Algeria;5. CONACYT—Centro de Investigación en Alimentación y Desarrollo, A.C., Consorcio CIDAM, A.C., Km. 8 Antigua Carretera a Pátzcuaro s/n, C.P. 58341, Morelia, Michoacán, Mexico;1. Department of Biocatalysis, Institute of Catalysis and Petrochemistry, Consejo Superior de Investigaciones Científicas (CSIC), 28049 Madrid, Spain;2. Department of Chemistry, Universidad de Guadalajara, 44430 Jalisco, Mexico;3. Department of Chemistry, Kharazmi University, 1417466191 Tehran, Iran;4. Pharmacy and Biotechnology Department, School of Biomedical Sciences, Universidad Europea de Madrid, Villaviciosa de Odón, 28670 Madrid, Spain;5. Laboratory of Microbiology and Food Biocatalysis, Institute of Food Science Research (CIAL, CSIC-UAM). Nicolás Cabrera, 9. UAM Campus, Cantoblanco, 28049, Madrid, Spain;1. Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC, Madrid, Spain;2. Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia;3. Laboratorio de Biotecnología Molecular, Instituto de Biotecnología Misiones “María Ebe Reca”, (FCEQyN–UnaM), Posadas, Argentina;4. Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, CEP 60455-760 Fortaleza, CE, Brazil;5. Departamento de Química, Facultad de Ciencias, Universidad del Tolima, Ibagué, Colombia;1. Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC 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), Universidad Industrial de Santander, Edificio Camilo Torres 210, Bucaramanga, Colombia;4. Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, CEP 62785-000 Acarape, CE, Brazil;5. Departamento de Química, Facultad de Ciencias. Universidad del Tolima, Ibagué, Colombia;6. Escuela de Microbiología, Universidad Industrial de Santander, Bucaramanga, Colombia;7. Istanbul Arel University, Faculty of Science and Letters, Department of Molecular Biology and Genetics, Tepekent, Buyukcekmece, Istanbul, Turkey;8. Yıldız Technical University, Graduate School of Natural and Applied Sciences, Department of Chemistry. Beşiktaş Merkez Yerleşkesi, Beşiktaş, Istanbul, Turkey;1. Deparatamento Biocatálisis. ICP-CSIC, Campus UAM-CSIC Madrid, Spain;2. Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Bloco 709, CEP 60455-760, Fortaleza, CE, Brazil;1. Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain;2. Transformation and Food Product Elaboration Laboratory, Nutrition and Food, Technology Institute (INATAA), University of Brothers Mentouri Constantine 1, Algeria;3. Laboratoire de Biotechnologies Végétales et Ethnobotanique, Faculté des Sciences de la Nature et de la Vie, Université de Bejaia, 06000, Bejaia, Algeria;4. Biotechnology, Bioprocess, and Biocatalysis Group, Food Science and Technology Institute, Federal University of Rio Grande do Sul, Porto Alegre, RS, Brazil;5. Group of Plant Proteins, Department of Food and Health, Instituto de la Grasa-CSIC, Seville, Spain;6. Center of Excellence in Bionanoscience Research, External Scientific Advisory Academics, King Abdulaziz University, Jeddah, 21589, Saudi Arabia |
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| Abstract: | A destabilizing effect at pH 7 of sodium phosphate on several lipases immobilized via interfacial activation is shown in this work. This paper investigates if this destabilizing effect is extended to other inactivation conditions, immobilization protocols or even other immobilized enzymes (ficin, trypsin, β-galactosidase, β-glucosidase, laccase, glucose oxidase and catalase). As lipases, those from Candida antarctica (A and B), Candida rugosa and Rhizomucor miehei have been used. Results confirm the very negative effect of 100 mM sodium phosphate at pH 7.0 for the stability of all studied lipases immobilized on octyl agarose, while using glutaraldehyde-support the effect is smaller (still very significant using CALA) and in some cases the effect disappeared (e.g., using CALB). The change of the pH to 5.0 or 9.0, or the addition of 1 M NaCl reduced the negative effect of the phosphate in some instances (e.g., at pH 5.0, this negative effect is only relevant for CALB). Regarding the other enzymes, only the monomeric β-galactosidase from Aspergillus oryzae is strongly destabilized by the phosphate buffer. This way, the immobilization protocol and the inactivation conditions strongly modulate the negative effect of sodium phosphate on the stability of immobilized lipases, and this effect is not extended to other enzymes. |
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| Keywords: | Immobilized enzyme stability Buffers and enzyme stability Tuning enzyme stability by immobilization Lipase interfacial activation Enzyme destabilization |
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