Improving the emulsification characteristics of rapeseed protein isolate by ultrasonication assisted pH shift treatment.

Int J Biol Macromol

School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, China; Institute of Food Physical Processing, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, China.

Published: December 2024

Rapeseed protein isolate (RPI) is an important nutrimental macronutrient in human diet due to its abundance in amino acids. However the poor emulsifying attributes of RPI limits its application in food industry, which needs to be overcome for its application in food industry. Ultrasonication-aided pH shift (UpHS) treatment is an efficient method for enhancing the functionality of plant/ food protein. In this work, the emulsification characteristics of RPI modified by UpHS technique under different solubility levels were studied. Results showed that the emulsifying activity and stability of modified RPI were significantly improved by 168.46 % (sample with high solubility treated by Ultrasonication-aided pH 12.5, HSpH 12.5) and 134.5 % (sample with high solubility treated by Ultrasonication-aided pH 1.5, HSpH 1.5), respectively compared with the native sample (P < 0.05), and the emulsifying activity was positively correlated (P < 0.05) with solubility. The emulsification stability under acidic condition was higher than that under alkaline condition (HSpH 12.5 increased by 83.5 %). In addition, the adsorption capacity and zeta potential of RPI were increased to 93.74 % and 13.83 % respectively, whereas the particle size and surface tension were reduced to 41.04 % and 23.63 % respectively. This indicates the changes in the molecular structure of modified rapeseed protein, which improved the emulsifying activity of RPI. Moreover, the interfacial film of emulsions formed by the modified protein had stronger compressive resistance, contributing to the enhanced emulsifying stability of the RPI. These results show that UpHS treatment can effectively improve the emulsification properties of proteins, and can be widely used in food industry.

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Source
http://dx.doi.org/10.1016/j.ijbiomac.2024.137221DOI Listing

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