Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads

Molecules

卷:22

Francisco A. Dias Filho¹  Telma L. G. Lemos¹  Roberto Fernández-Lafuente²  Ana D. Q. Melo³  Francisco F. M. Silva⁴  José C. S. dos Santos⁵ 

[1] Departamento de Química Orgânica e Inorgânica da Universidade Federal do Ceará, Campus do Pici, Bloco 940, Fortaleza CEP 60455-760, Ceará, Brazil;

[2] Department of Biocatalysis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain;

[3] Instituto Federal de Educação, Ciência e Tecnologia do Ceará, Rod. Pres. Juscelino Kubitschek, Boa Viagem CEP 63870-000, Ceará, Brazil;

[4] Instituto Federal de Educação, Ciência e Tecnologia do Rio Grande do Norte, RN 233, Km-02, Nº 999, Bairro Chapada do Apodi, Apodi CEP 59700-000, Rio Grande do Norte, Brazil;

[5] Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, Redenção CEP 62785-000, Ceará, Brazil;

关键词: chitosan;    polyphosphate;    microspheres;    immobilization;    lipase;    CALB;   

DOI  :  10.3390/molecules22122165

来源: DOAJ

【 摘 要 】

Enzymes serve as biocatalysts for innumerable important reactions, however, their application has limitations, which can in many cases be overcome by using appropriate immobilization strategies. Here, a new support for immobilizing enzymes is proposed. This hybrid organic-inorganic support is composed of chitosan—a natural, nontoxic, biodegradable, and edible biopolymer—and sodium polyphosphate as the inorganic component. Lipase B from Candida antarctica (CALB) was immobilized on microspheres by encapsulation using these polymers. The characterization of the composites (by infrared spectroscopy, thermogravimetric analysis, and confocal Raman microscopy) confirmed the hybrid nature of the support, whose external part consisted of polyphosphate and core was composed of chitosan. The immobilized enzyme had the following advantages: possibility of enzyme reuse, easy biocatalyst recovery, increased resistance to variations in temperature (activity declined from 60 °C and the enzyme was inactivated at 80 °C), and increased catalytic activity in the transesterification reactions. The encapsulated enzymes were utilized as biocatalysts for transesterification reactions to produce the compound responsible for the aroma of jasmine.

【 授权许可】

Unknown