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| Process optimization of enzymatic modification of octanoic acid-structured soybean phospholipids |
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| DOI：10.19902/j.cnki.zgyz.1003-7969.230099 |
| KeyWord:soybean phospholipids lipase fatty acid enzymatic modification structured phospholipids |
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| Abstract: |
| In order to improve the physicochemical properties of natural phospholipids as well as to expand their applications, soybean phospholipids were modified by an enzymatic method using octanoic acid and soybean phospholipids as substrates. Lipases for modifying soybean phospholipids were screened, and the effects of reaction temperature, reaction time, lipase dosage and substrate mass ratio on the modification process of octanoic acid-structured soybean phospholipids were investigated. On this basis, orthogonal tests were used to optimize the process conditions of the enzyme-catalyzed modification of soybean phospholipids, and the reusability of the lipases was determined. The results showed that the catalytic effect of Novozym 435 was stronger than that of Lipozyme RM IM and Lipozyme TL IM. The optimal conditions for the enzyme-catalyzed modification of soybean phospholipids were reaction temperature 55 ℃, Novozym 435 dosage 25%, mass ratio of octanoic acid to soybean phospholipids 7∶ 1, and reaction time 36 h. The octanoic acid binding rate was (78.79±0.81)% under the optimal conditions, and the octanoic acid binding rate still reached (63.67±1.50)% after four times of reuse of Novozym 435. In conclusion, Novozym 435 can be used as a preferred lipase to catalyze the modification of phospholipids. |
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