Ball-milling changed the physicochemical properties of SPI and its cold-set gels

July 28, 2017

Title

Ball-milling changed the physicochemical properties of SPI and its cold-set gels

Author

Bohui Liu, Hui Wang, Tan Hu, Peipei Zhang, Zhuo Zhang, Siyi Pan, Hao Hu

Year

2016

Journal

Journal of Food Engineering

Abstract

In this study, the effect of ball-milling (BM, Mixer Mill MM 400) treatments on the physicochemical properties of soybean protein isolate (SPI) and its cold-set gels induced by glucono-δ-lactone was studied. BM of SPI increased the gel strength and water holding capacity of cold-set gels significantly after 4 min of BM treatments. BM treatments did not alter the primary structure of SPI, but caused minor changes of the secondary structure. Furthermore, surface hydrophobicity of SPI increased gradually from 2058 to 5051 after 10 min of BM, while free SH groups reduced from 3.92 to 2.65 μmol/g protein. Moreover, near-UV CD spectra indicated that the tertiary conformation stability was increased and the hydrophobic groups might shift to a more hydrophobic microenvironment. In conclusion, appropriate BM treatments could change the physicochemical properties of SPI and increased the gelation properties of SPI cold-set gels.

Instrument

J-1500

Keywords

Circular dichroism, Secondary structure, Tertiary structure, Biochemistry, Food science