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Influence of stewing conditions on tenderness and protein structure in beef
Author(s) -
Wan Hongbing,
Li Haipeng,
Lei Yuanhua,
Xie Peng,
Zhang Songshan,
Wang Huan,
Liu Xuan,
Sun Baozhong
Publication year - 2021
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/jfpp.15208
Subject(s) - tenderness , myofibril , chemistry , myosin , food science , longissimus dorsi , biochemistry
In this study, the effects of heating temperature (70°C ~ 100°C) and time (0 ~ 180 min) on beef M. longissimus dorsi tenderness, the oxidation characteristics of myofibrillar protein (MP), and the correlation between tenderness with protein oxidation characteristics were studied. The results showed that heating temperature and time significantly influenced beef tenderness and MP oxidation characteristics. SDS‐PAGE analysis indicated that the thermal stability of actin was significantly higher than that of myosin heavy chain. Myosin heavy chain bands disappeared completely when heated for 120 min at 90°C or for 30 min at 100°C. The actin bands faded slightly and they were still clearly visible when heated for 180 min at 100°C. Correlation analysis showed that beef shear force value was significant negatively correlated with the dityrosine content ( p < .01). This will provide a theoretical basis for the quality control and cooking process optimization of Chinese traditional beef stew dishes. Novelty impact statement This study investigated the changes of beef tenderness and myofibrillar protein structure during stewing and elucidated the correlation between beef tenderness and myofibrillar protein structure. The results will provide a theoretical basis for the quality control and cooking process optimization of Chinese traditional beef stew dishes.