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Effects of Reaction Operation Policies on Properties of Core–Shell Polymer Supports Used for Preparation of Highly Active Biocatalysts
Authors:Martina Costa Cerqueira Pinto  Nathany Lisbôa de Souza e Castro  Eliane Pereira Cipolatti  Roberto Fernandez‐Lafuente  Evelin Andrade Manoel  Denise Maria Guimarães Freire  José Carlos Pinto
Institution:1. Programa de Engenharia Química, COPPE, Universidade Federal do Rio de Janeiro, 68502 Rio de Janeiro, Brazil;2. Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, 21941‐909 Rio de Janeiro, BrazilE‐mail: ,;3. Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, 21941‐909 Rio de Janeiro, Brazil;4. Department of Biocatalysis, ICP‐CSIC, Campus UAM‐CSIC, Cantoblanco, 28049 Madrid, Spain;5. Departamento de Biotecnologia Farmacêutica, Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, 21941‐902 Rio de Janeiro, Brazil;6. Programa de Engenharia Química, COPPE, Universidade Federal do Rio de Janeiro, 68502 Rio de Janeiro, BrazilE‐mail: ,
Abstract:Core–shell polymer supports with different morphological features and compositions are prepared through combined suspension and emulsion polymerizations. It is shown that proper manipulation of the divinylbenzene (DVB) feed content allows for maximization of specific areas, porosities, and mechanical resistances. Additionally, it is shown that feeding of previously prepared miniemulsions leads to core–shell particles with smaller specific areas, due to less efficient coating of the cores. Particularly, the combined manipulation of polymerization times and DVB feed compositions allows for production of particles with pronounced specific area (50 m2 g?1) and porosity (0.30 cm3 g?1). Produced core–shell polymer particles are employed as supports for the immobilization of lipase B from Candida antarctica, and the obtained enzymatic activities for both hydrolysis (A hyd) and esterification (A est) reactions are very high (A hyd = 34.7 ± 3.8 U/g; A est = 3564.6 ± 581 U/g), even when compared to activities obtained using the reference commercial biocatalyst Novozym 435 (A hyd = 7.6 ± 1.8 U/g, A est = 2384.7 ± 307.2 U/g). Finally, biocatalysts prepared with the core–shell supports present higher enzymatic activities than biocatalysts prepared with supports of higher specific area obtained through conventional emulsion polymerizations, indicating that the porous structure of the shell can be beneficial for the immobilization and activity of the enzymes.
Keywords:biocatalyst  combined suspension and emulsion polymerization  core–  shell particles  immobilization  lipase B from Candida antarctica   
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