| Autor: |
Guiyan Li, Xiang Zuo, Xinlin Luo, Zhongqin Chen, Wenhong Cao, Haisheng Lin, Xiaoming Qin, Leiyan Wu, Huina Zheng |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Food Chemistry: X, Vol 19, Iss , Pp 100841- (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2590-1575 |
| DOI: |
10.1016/j.fochx.2023.100841 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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