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

Autor: Francisco Felipe Maia da Silva, Ana D.Q. Melo, José C. S. dos Santos, Roberto Fernandez-Lafuente, Francisco A. Dias Filho, Telma L. G. Lemos
Jazyk: angličtina
Rok vydání: 2017
Předmět:
Pharmaceutical Science
02 engineering and technology
01 natural sciences
Analytical Chemistry
Microsphere
Chitosan
chemistry.chemical_compound
Polyphosphates
Drug Discovery
Organic chemistry
organic_chemistry
Candida
biology
021001 nanoscience & nanotechnology
CALB
Microspheres
Chemistry (miscellaneous)
Molecular Medicine
0210 nano-technology
Immobilized enzyme
Article
Catalysis
lcsh:QD241-441
Fungal Proteins
lcsh:Organic chemistry
Benzyl Compounds
Physical and Theoretical Chemistry
Lipase
Esterification
010405 organic chemistry
Polyphosphate
Spectrum Analysis
Organic Chemistry
polyphosphate
biology.organism_classification
equipment and supplies
Enzymes
Immobilized
0104 chemical sciences
Benzyl acetate
chemistry
Biocatalysis
chitosan
microspheres
immobilization
lipase
biology.protein
Candida antarctica
Adsorption
Nuclear chemistry
Zdroj: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules, Vol 22, Iss 12, p 2165 (2017)
Molecules; Volume 22; Issue 12; Pages: 2165
ISSN: 1420-3049
Popis: Enzymes serve as biocatalysts for innumerable important reactions; however, their application has limitations, which could 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, which was the inorganic component. Lipase B from Candida antarctica (CALB) was immobilized in 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.
Databáze: OpenAIRE
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