Solubility, Free Amino and Freeze-Thaw Stability of Soy Protein Isolated Prepared by Papain Modification

DOI

10.2991/meep-15.2016.48How to use a DOI?

Keywords

soy protein isolate; papain; freeze-thaw stability; protein solubility; free amino groups

Abstract

Peptide size control is important for obtaining desirable functional properties so that these peptides can be better utilized. Proteolytic enzyme modification of soy protein isolates (SPI) is an effective way to fractionate these proteins into peptides with controlled molecular size. SPI was partial hydrolysis by papain at pH 7.0 and 50°C. Protein solubility, free amino groups, and freeze-thaw stability of the control SPI (without added papain) and hydrolysates were investigated. Hydrolysates that were prepared from SPI by papain modification had higher solubility, and better freeze-thaw stability. They could find use in products that require these Properties.

Copyright

© 2016, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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TY  - CONF
AU  - M.J. Liu
AU  - G.P. Yu
AU  - Y.X. Yao
AU  - P.P. Guo
AU  - W.W. Qi
AU  - X.H. Cai
PY  - 2016/03
DA  - 2016/03
TI  - Solubility, Free Amino and Freeze-Thaw Stability of Soy Protein Isolated Prepared by Papain Modification
BT  - Proceedings of the 2015 International Conference on Materials Chemistry and Environmental Protection (meep-15)
PB  - Atlantis Press
SP  - 182
EP  - 185
SN  - 2352-541X
UR  - https://doi.org/10.2991/meep-15.2016.48
DO  - 10.2991/meep-15.2016.48
ID  - Liu2016/03
ER  -