Immobilization of lipase on porous monodisperse chitosan microspheres

Chen, Yang; Liu, Junteng; Xia, Chunjie; Zhao, Chenxi; Ren, Zhongqi; Zhang, Weidong

doi:10.1002/bab.1242

Cited by 12 publications

(3 citation statements)

References 32 publications

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“…Some scientists 17) demonstrated the synthesis of capecitabine-loaded semi-IPN hydrogel microspheres of chitosan-poly (ethylene oxideg-acrylamide) using GA and HCl solution. NaOH solution and GA solution also could be used as the cross-linkers by emulsion crosslinking method 18,19) . In our delivery system, vanillin and vitriolic acid were used as double cross-linkers.…”

Section: Discussionmentioning

confidence: 99%

Research on a novel chitosan microsphere/scaffold system by double crosslinkers

Zhou

Tai

et al. 2016

Dent. Mater. J.

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RhBMP-2 has shown great promise for the reconstruction of teeth segmental bone defects due to its osteoinductive properties. But the application of rhBMP-2 is limited by its weak drug controled release. It is usually loaded in a Chitosan Microspheres (CMs) delivery system with excess single cross-linker and then removed before practice. In this study, cross-linkers were replaced with RhBMP-2 which contains vanillin and vitriolic acid, and thus CMs were developed. The materials were studied by SEM, FTIR and drug release experiments. It showed an ideal releasing profile and excellent osteoconductive and osteoinductive performance in the delivery system. Therefore, designing biomaterials with a controllable delivery system composite and releasing profile of rhBMP-2 are critical for applications of bone regeneration and tissue engineering.

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Section: Discussionmentioning

confidence: 99%

Research on a novel chitosan microsphere/scaffold system by double crosslinkers

Zhou

Tai

et al. 2016

Dent. Mater. J.

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“…The systems stored at 4 • C, after the analyzed time period, retain almost all of their original activity (96%), while immobilized lipase stored at 20 • C shows a decline in activity by approximately 10%. Chen et al [69] reported activity of lipase immobilized on chitosan microspheres at levels of 80% and 60% after storage at 4 • C for 5 and 20 days, respectively. Meanwhile Zhu et al [70] found that lipase immobilized on silica-coated magnetic nanoparticles preserved 70% of its initial activity after 20 days, when stored at 20 • C. The results obtained in our research indicate that immobilization of Candida antarctica lipase B on a silica-lignin support significantly extends its catalytic activity compared with the free enzyme and with previously published results.…”

Section: Storage Stabilitymentioning

confidence: 99%

Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System

et al. 2016

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A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM), as well as the determination of changes in porous structure parameters, confirmed the effective immobilization of the enzyme on the surface of the composite matrix. Based on a hydrolysis reaction, a determination was made of the retention of activity of the immobilized lipase, found to be 92% of that of the native enzyme. Immobilization on a silica-lignin matrix produces systems with maximum activity at pH = 8 and at a temperature of 40 • C. The immobilized enzyme exhibited increased thermal and chemical stability and retained more than 80% of its activity after 20 reaction cycles. Moreover immobilized lipase exhibited over 80% of its activity at pH range 7-9 and temperature from 30 • C to 60 • C, while native Candida antarctica lipase B (CALB) exhibited the same only at pH = 7 and temperature of 30 • C.

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“…Chitin is normally isolated from the exoskeletons of many species of insects and crustaceans [ 34 ]. Furthermore, chitosan is a biocompatible gel-forming cationic compound that can readily be prepared in different geometrical configurations, such as membranes, beads, nanoparticles by nano-immobilization [ 35 ], fibers, hollow fibers or sponges [ 15 , 36 , 37 , 38 , 39 ].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2017

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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.

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Immobilization of lipase on porous monodisperse chitosan microspheres

Cited by 12 publications

References 32 publications

Research on a novel chitosan microsphere/scaffold system by double crosslinkers

Research on a novel chitosan microsphere/scaffold system by double crosslinkers

Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System

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

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