Study on the stability of intermediates in the process of enzymatic hydrolysis of phosphatidic acid by phospholipase A1.

In the degumming process of crude soybean oil by phospholipase A 1 (PLA 1), the content of free fatty acids (FFA) in the product increases excessively. In this study, PLA 1 was used to hydrolyse simulated crude soybean oil. It was found that the acyl group at the s n- 2 position migrated to the s n- 1 position, the content of FFA in the oil was as high as 1.26 ± 0.03 g/100 g, and the acyl migration rate was up to 38.9 ± 0.10% after 2.8 h. Under the conditions of H 3 BO 3 addition of 2 g/100 g, pH of 5, enzymatic hydrolysis temperature of 50 °C and enzymatic hydrolysis time of 2 h, the acyl migration rate of s n- 2-HPA was 16.8 ± 0.50%, the content of FFA was 1.14 ± 0.02 g/100 g, and the enzymatic hydrolysis efficiency was increased by 28.57 ± 0.07%. • Sn- 2-HPA is unstable, forms a five-membered ring intermediate, cause acyl migration. • Lone pair electron at s n- 1 site is a key factor affecting the stability of s n- 2-HPA. • H 3 BO 3 forms coordination bond with s n- 1 site, blocking the formation of intermediate. • By adding 2% H 3 BO 3 , FFA content was reduced, enzymolysis efficiency was improved. [ABSTRACT FROM AUTHOR]