Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads.
Ana D Q MeloFrancisco F M SilvaJosé Cleiton Sousa Dos SantosRoberto Fernández-LafuenteTelma L G LemosFrancisco A Dias FilhoPublished in: Molecules (Basel, Switzerland) (2017)
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.
Keyphrases
- drug delivery
- ionic liquid
- wound healing
- magnetic nanoparticles
- hyaluronic acid
- optical coherence tomography
- water soluble
- capillary electrophoresis
- high resolution
- raman spectroscopy
- wastewater treatment
- single molecule
- room temperature
- escherichia coli
- label free
- mass spectrometry
- gold nanoparticles
- cystic fibrosis
- molecularly imprinted
- aqueous solution