Version 1
: Received: 9 August 2017 / Approved: 10 August 2017 / Online: 10 August 2017 (05:44:58 CEST)
How to cite:
Felipe Maia da Silva, F.; Melo, A.D.; Lemos, T.L.; Dias Filho, F.A.; Sousa, C.; Fernandez-Lafuente, R. Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads. Preprints2017, 2017080038 (doi: 10.20944/preprints201708.0038.v1).
Felipe Maia da Silva, F.; Melo, A.D.; Lemos, T.L.; Dias Filho, F.A.; Sousa, C.; Fernandez-Lafuente, R. Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads. Preprints 2017, 2017080038 (doi: 10.20944/preprints201708.0038.v1).
Cite as:
Felipe Maia da Silva, F.; Melo, A.D.; Lemos, T.L.; Dias Filho, F.A.; Sousa, C.; Fernandez-Lafuente, R. Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads. Preprints2017, 2017080038 (doi: 10.20944/preprints201708.0038.v1).
Felipe Maia da Silva, F.; Melo, A.D.; Lemos, T.L.; Dias Filho, F.A.; Sousa, C.; Fernandez-Lafuente, R. Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads. Preprints 2017, 2017080038 (doi: 10.20944/preprints201708.0038.v1).
Abstract
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.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Francisco Felipe Maia da Silva
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