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Updated: Jul 8, 2025

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Preparation of magnetic dialdehyde starch-immobilized phospholipase A1 and acyl transfer in reflection
Yawen Wang1, Ning Wang1, Peng Wang1
1School of Food Science, Northeast Agricultural University, Harbin 150030, China.
Abstract:
In this paper, using a coprecipitation method to prepare Fe3O4 magnetic nanoparticles (Fe3O4 MNPS), magnetic dialdehyde starch nanoparticles with immobilized phospholipase A1 (MDSNIPLA) were successfully prepared by using green dialdehyde starch (DAS) instead of glutaraldehyde as the crosslinking agent. The Fe3O4 MNPS was characterized by infrared spectroscopy (FT-IR), scanning electron microscopy (SEM), the Brunauer-Emmett-Teller (BET) surface area analysis method, thermogravimetric analysis (TGA), and transmission electron microscopy (TEM) et al. The results showed that the alkaline resistance and acid resistance of the enzyme were improved after the crosslinking of DAS. After repeated use (seven times), the relative activity of MDSNIPLA reached 56 %, and the magnetic dialdehyde starch nanoparticles (MDASN) had good carrier performance. MDSNIPLA was applied to enzymatic hydrolysis of phospholipids in the soybean oil degumming process. The results showed that the acyl transfer rate of sn-2-HPA was 14.01 %, and the content of free fatty acids was 1.144 g/100 g after 2 h reaction at 50 °C and pH 5.0 with appropriate boric acid. The immobilized enzyme has good thermal stability and storage stability, and its application of soybean oil improves the efficiency of the oil.
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