酯交换脂肪
脂肪酶
化学
皱纹假丝酵母
介孔材料
固定化酶
甘油三酯酶
色谱法
有机化学
催化作用
酶
作者
Junxin Zhao,Maomao Ma,Xianghui Yan,Guohua Zhang,Jiaheng Xia,Zheling Zeng,Ping Yu,Qiang Deng,Deming Gong
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2022-01-15
卷期号:379: 132148-132148
被引量:35
标识
DOI:10.1016/j.foodchem.2022.132148
摘要
In this study, the polydopamine functionalized magnetic mesoporous biochar (MPCB-DA) was prepared for immobilization of Bacillus licheniformis lipase via covalent immobilization. Under optimized immobilization conditions, the maximum immobilization yield, efficiency and immobilized lipase amount were found to be 45%, 54% and 36.9 mg/g, respectively. The immobilized lipase, MPCB-DA-Lipase showed good thermal stability and alkali resistance. The MPCB-DA-Lipase retained 56% initial activity after 10 reuse cycles, with more than 85% relative activity after 70 days' storage at 4 or 25 °C. The MPCB-DA-Lipase was efficiently applied in the interesterification of Cinnamomum camphora seed kernel oil and perilla seed oil, with maximum interesterification efficiency of 46%. The produced structured lipids belong to the S2U and U2S triacylglycerols, a novel medium-and long-chain triacylglycerol. These results demonstrated that the MPCB-DA-Lipase may be used as an efficient biocatalyst in lipid processing applications of food industries.
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