Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10129225 | International Journal of Biological Macromolecules | 2018 | 32 Pages |
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 6100.00â¯Â±â¯246.41â¯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 70â¯Â°C. 1-isocyanatopropane group modified SBA-15 supported CALB exhibited selectivity for DAG production. DAG content up to 61.90â¯Â±â¯2.38â¯wt% and a DAG/MAG ratio at 3.11â¯Â±â¯0.08 was obtained after a 24-h reaction at 60â¯Â°C in a solvent-free system.
Keywords
Related Topics
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Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Yue Li, Nanjing Zhong, Ling-Zhi Cheong, Jianrong Huang, Hongxiao Chen, Shaoyan Lin,