location: Current position: Home >> Scientific Research >> Paper Publications

Esterification degree of fructose laurate exerted by Candida antarctica lipase B in organic solvents

Hits:

Indexed by:期刊论文

Date of Publication:2015-02-01

Journal:ENZYME AND MICROBIAL TECHNOLOGY

Included Journals:SCIE、EI、PubMed、Scopus

Volume:69

Page Number:46-53

ISSN No.:0141-0229

Key Words:Sugar ester of fatty acid; Degree of esterification; Candida antarctica lipase B; Fructose laurate; ATR-FTIR

Abstract:Sugar esters of fatty acids have many applications as biocompatible and biodegradable emulsifiers, which are determined by their degrees of esterification (DE). Direct esterification of fructose with lauric acid in organic media used commercial immobilized Candida antarctica lipase B (CALB) was investigated for DE. Significant difference of DE was observed between 2-methyl-2-butanol (2M2B) and methyl ethyl ketone (MEK), as di-ester/mono-ester molar ratio of 1.05:1 in 2M2B and 2.79:1 in MEK. Fourier transform infrared (FTIR) spectra showed that the secondary structure of the enzyme binding mono-ester presented distinct difference in 2M2B and MEK. Contents of beta-turn and antiparallel beta-sheet of CALB in 2M2B were 26.9% and 16.2%, respectively, but 19.1% and 13.2% in MEK. To understand the relationship between the conformational changes and differences of DE, mono-ester and fatty acid were directly employed for synthesis of di-ester. The maximum initial velocity of di-ester synthesis in MEK was 0.59 mmol g(enzyme)(-1) h(-1), which was 2.19-fold as greater as that in 2M2B, indicating that CALB conformation in MEK was preferred for the synthesis of di-ester. These results demonstrated that the conformation of CALB binding mono-ester affected by organic solvents essentially determined DE. (C) 2014 Elsevier Inc. All rights reserved.

Pre One:Ratiometric Fluorescence Imaging of Cellular Polarity: Decrease in Mitochondrial Polarity in Cancer Cells

Next One:A Nile blue based infrared fluorescent probe: imaging tumors that over-express cyclooxygenase-2