水解物
木瓜蛋白酶
鲍鱼
盘鲍
化学
乳状液
水解
食品科学
酶水解
功能性食品
溶解度
色谱法
生物化学
酶
渔业
生物
有机化学
作者
Guiyan Li,Xiaoxia Zuo,X. L. Luo,Zhongqin Chen,Wenhong Cao,Haisheng Lin,Xiaoming Qin,Leiyan Wu,Huina Zheng
标识
DOI:10.1016/j.fochx.2023.100841
摘要
This study was conducted to investigate functional, physicochemical, and structural properties of abalone foot muscle proteins (AFPs) and their hydrolysates (HAFPs) obtained using animal protease (HA), papain (HPP), and Protamex® (HP) at different time points. The HA-hydrolysate obtained after 0.5 h of treatment demonstrated the highest solubility at pH 7.0 (84.19%); the HPP-hydrolysate at 4 h exhibited the highest degree of hydrolysis (11.4%); the HPP-hydrolysate at 0.5 h had the highest oil holding capacity (2.62 g/g) and emulsion stability index (39.73 min), and the HP-hydrolysate at 4 h had the highest emulsifying activity index (93.23 m2/g) and foaming stability (91.45%); Regarding the physicochemical properties, the HPP-hydrolysates revealed the largest particle size, higher absolute zeta potential, and superior interfacial activity. Structural characterization demonstrated the enzymolysis-based changes in the composition and the secondary structure of the AFPs. These results provide practical support for the theoretical basis of the use of AFPs as a source of nutritive proteins in the food industry.
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