期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 60, 期 10, 页码 2569-2576出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf205280y
关键词
meat protein; oxidation; aggregation; in vitro digestion; processing
资金
- French Research National Agency [ANR-09-ALIA-008-01]
- European fund for regional development (FEDER)
- Auvergne regional council
The present study aimed to evaluate the digestion rate and nutritional quality of pig muscle proteins in relation to different meat processes (aging, mincing, and cooking). Under our experimental conditions, aging and mincing had little impact on protein digestion. Heat treatments had different temperature-dependent effects on the meat protein digestion rate and degradation potential. At 70 degrees C, the proteins underwent denaturation that enhanced the speed of pepsin digestion by increasing enzyme accessibility to protein cleavage sites. Above 100 degrees C, oxidation-related protein aggregation slowed pepsin digestion but improved meat protein overall digestibility. The digestion parameters defined here open new insights on the dynamics governing the in vitro digestion of meat protein. However, the effect of cooking temperature on protein digestion observed in vitro needs to be confirmed in vivo.
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