Effects of Sequential Enzymolysis and Glycosylation on the Structural Properties and Antioxidant Activity of Soybean Protein Isolate

The effects of limited hydrolysis following glycosylation with dextran on the structural properties and antioxidant activity of the soybean protein isolate (SPI) were investigated. Three SPI hydrolysate (SPIH) fractions, F30 (>30 kDa), F30-10 (10-30 kDa), and F10 (<10 kDa), were confirmed using gel permeation chromatography. The results demonstrated that the glycosylation of F30 was faster than that of F30-10 or F10. The enzymolysis caused the unfolding of the SPI to expose the internal hydrophobic cores, which was further promoted by the grafting of dextran, making the obtained conjugates have a loose spatial structure, strong molecular flexibility, and enhanced thermal stability. The grafting of dextran significantly enhanced the DPPH radical or center dot OH scavenging activity and the ferrous reducing power of the SPI or SPIH fractions with different change profiles due to their different molecular structures. The limited enzymolysis following glycosylation was proven to be a promising way to obtain SPI-based food ingredients with enhanced functionalities.

Automated summary

This study investigated the effects of limited hydrolysis following glycosylation with dextran on the structural properties and antioxidant activity of soybean protein isolate (SPI). Three SPI hydrolysate fractions were confirmed using gel permeation chromatography. The results showed that glycosylation of larger SPI fragments was faster and the enzymolysis caused the unfolding of SPI and exposed hydrophobic cores. The grafting of dextran enhanced the spatial structure, molecular flexibility, thermal stability, DPPH radical and center dot OH scavenging activity, and ferrous reducing power of the SPI or SPIH fractions with different molecular structures.