Functional, physicochemical, and structural properties of the hydrolysates derived from the abalone (Haliotis discus subsp hannai Ino) foot muscle proteins.

ABSTRACT: 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, high

SUBMITTER: Li G 

PROVIDER: S-EPMC10481181 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature