Abstract
The effects of molecular weight (MW) and degree of esterification (DE) of soluble soybean polysaccharide (SSPS) on the stability of casein under acidic conditions were investigated. The ability of SSPS to stabilize casein was characterized by the content of SSPS–casein complex, the LUMiSizer instability index, average particle size, zeta potential, and storage experiments. The long-term storage stability of the mixtures was related to their ability to combine casein and the stability of the complexes. At the same DE, SSPSs with medium MW formed more complexes with casein than SSPSs with high or low MW; and at the same MW, SSPSs with medium or low DE formed more complexes than SPSSs with high DE. In addition, SSPSs with higher MW had a better stabilizing behavior due to the large steric repulsion between complexes. SSPSs with high MW and low DE showed the best ability to stabilize casein under acid conditions.
Highlights
Acidified milk drinks are a series of beverages produced by dilution, acidification, and homogenization, such as yogurt drinks, milk drinks with fruit, buttermilk, and whey drinks [1,2,3,4,5]
After de-esterification, the molecular weight (MW) of high DE (HH) (1.42 × 106 Da) decreased from 1.42 × 106 Da to 1.15 × 106 Da (HM) and 1.06 × 106 Da (HL), Foods 2021, 10, x FOR PEER REVIEW which demonstrated that both the degree of esterification (DE) and MW of SSPS decreased during de-esterifi6caotfio1n4
LL formed most complexes and showed the lowest instability index at this ratio (Sections 3.2 and 3.3.2). These results indicated that SSPS–casein complexes can prevent the aggregation of casein, which resulted in a more uniform particle size distribution and smaller mean particle diameter
Summary
Acidified milk drinks are a series of beverages produced by dilution, acidification, and homogenization, such as yogurt drinks, milk drinks with fruit, buttermilk, and whey drinks [1,2,3,4,5]. Another study reported that a new SSPS with higher MW (2.85 × 106 Da) could stabilize acidified milk drinks better than SSPS with a lower MW (5.5 × 105 Da), and this was mainly due to the larger steric repulsion formed by complexes [14]. Xiong et al (2015) found that the ability of SSPS to stabilize proteins increased as the DE value decreased from 83% to 49%, and SSPS with both lower DE and lower MW had better stabilizing ability [34] These inconsistent results suggest that the mechanism of SSPS stabilizing acidified casein is still not clear, and the influence of structural factors such as MW and DE on the complexes needs to be explored further. The ability of SSPS with different MWs and DEs to stabilize casein was analyzed by the instability index, complex content, average particle size, zeta potential, and storage experiments
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
