Solubility, Free Amino and Freeze-Thaw Stability of Soy Protein Isolated Prepared by Papain Modification
M.J. Liu, G.P. Yu, Y.X. Yao, P.P. Guo, W.W. Qi, X.H. Cai
Available Online March 2016.
- https://doi.org/10.2991/meep-15.2016.48How to use a DOI?
- soy protein isolate; papain; freeze-thaw stability; protein solubility; free amino groups
- 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.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
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 - https://doi.org/10.2991/meep-15.2016.48 ID - Liu2016/03 ER -