Format

Send to

Choose Destination
Int J Biol Macromol. 2018 Dec;120(Pt A):886-895. doi: 10.1016/j.ijbiomac.2018.08.155. Epub 2018 Aug 30.

Immobilization of Candida antarctica Lipase B onto organically-modified SBA-15 for efficient production of soybean-based mono and diacylglycerols.

Author information

1
School of Food Science, Guangdong Pharmaceutical University, Zhongshan 528458, China.
2
School of Food Science, Guangdong Pharmaceutical University, Zhongshan 528458, China. Electronic address: adong473@163.com.
3
Department of Food Science and Engineering, College of Food and Pharmaceutical Sciences, Ningbo University, China.

Abstract

In this study, SBA-15 was modified by a series of silane coupling reagents and later used to immobilize Candida antartica lipase B (CALB). The enzymatic properties of the immobilized CALB samples were studied. In addition, the catalytic performance in glycerolysis of soybean oil for diacylglycerols (DAG) production was also investigated. The highest enzymatic activity up to 6100.00 ± 246.41 U/g was observed from the propyl methacrylate group modified SBA-15 supported CALB. No loss of activity was observed from the propyl methacrylate group modified SBA-15 supported CALB, but a higher-than-initial activity was notably found from 3-aminopropyl group and n-octyl group modified SBA-15 supported CALB after a 4-h incubation in air at 70 °C. 1-isocyanatopropane group modified SBA-15 supported CALB exhibited selectivity for DAG production. DAG content up to 61.90 ± 2.38 wt% and a DAG/MAG ratio at 3.11 ± 0.08 was obtained after a 24-h reaction at 60 °C in a solvent-free system.

KEYWORDS:

Candida antartica lipase B; Glycerolysis; Immobilization; Organic modification; SBA-15

PMID:
30172818
DOI:
10.1016/j.ijbiomac.2018.08.155
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center