Abstract: The digestibility of myofibrillar proteins (MP) extracted from yak meat cooked to different internal temperatures of (40, 50, 60, 70 and 80 ℃) was determined during in vitro gastrointestinal digestion, and total carbonyl content, total sulfhydryl content and Schiff base content before and after digestion were measured. Ultraviolet (UV) absorption spectroscopy, endogenous fluorescence spectroscopy and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) were used to investigate the oxidation and digestion patterns of yak meat proteins during gastrointestinal digestion. The results showed that total protease hydrolysis of MP from yak meat cooked to 60 ℃ was the highest after simulated gastric and intestinal digestion (88.64%). The rates of pepsin hydrolysis and total protease hydrolysis of MP from yak meat cooked to 80 ℃ decreased by 34.10% and 22.47%, respectively, and the rate of trypsin hydrolysis increased by 75.34% compared with MP from raw yak meat. The total carbonyl content after simulated gastric and intestinal digestion increased by 81.42% and 77.40%, respectively, and the total sulfhydryl content decreased by 30.02% and 36.43%, respectively, compared with raw MP. With an increase in cooking temperature, the Schiff base content gradually increased, the UV absorbance was significantly enhanced, and the endogenous fluorescence intensity was significantly reduced. The SDS-PAGE patterns showed that the protein bands were severely degraded and even disappeared after digestion. It was found that the digestibility of MP from yak meat cooked to 60 ℃ was the highest. The degree of protein oxidation in yak meat cooked to 80 ℃ was the strongest and increased during gastrointestinal digestion.

Key words: yak meat; cooking temperature; protein oxidation; digestibility