The dynamic change in the degradation and in vitro digestive properties of porcine myofibrillar protein during freezing storage.

The myofibrillar protein (MP) degradation and in vitro digestive properties of porcine longissimus during freezing at -8, -18, -25 and - 40 °C for 1, 3, 6, 9 and 12 months were investigated. As the freezing temperature and duration of frozen storage increased, the amino nitrogen and TCA (trichloroacetic acid)-soluble peptides of the samples were significantly increased, while the total sulfhydryl content and band intensity of myosin heavy chain, actin, troponin T, tropomyosin were significantly decreased (P < 0.05). At higher freezing storage temperatures and durations, the particle size of MP samples and the green fluorescent spots detected using a laser particle size analyzer and confocal laser scanning microscopy became large. After 12 months of freezing, the digestibility and the degree of hydrolysis of the trypsin digestion solution of the samples frozen at -8 °C were significantly decreased by 15.02 % and 14.28 %, respectively, when compared to fresh samples, whereas, the mean surface diameter (d) and mean volume diameter (d) were significantly increased by 14.97 % and 21.53 %, respectively. Therefore, frozen storage induced protein degradation and impaired the ability of digestion in the pork proteins. This phenomenon was more evident as the samples were frozen at high temperatures over a long storage period.