Journal
JOURNAL OF FOOD ENGINEERING
Volume 195, Issue -, Pages 158-165Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.jfoodeng.2016.10.006
Keywords
Mixer ball milling; Conformational structure; Soy protein; Cold-set gel; Gelation property; Particle size
Categories
Funding
- NSFC [31501406]
- Natural Science Foundation of Hubei Province of China [2015CFB246]
- Fundamental Research Funds for the Central Universities [2662015QC013]
Ask authors/readers for more resources
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-delta-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 mu mol/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. (C) 2016 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available