Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin.

Heat treatment affects the structural properties of meat proteins, which in turn leads to changes in their sensitivity to digestive enzymes, further affecting the nutritional value of meat and meat products. The mechanism of changes in the structure and digestive properties of myosin under different heating conditions were studied. An increase in heating temperature led to the exposure of internal groups to a polar environment, but to a decrease in the sturdy α-helix structure of myosin ( < 0.

Overheating induced structural changes of type I collagen and impaired the protein digestibility.

Collagen, especially type I collagen, a major component for connective tissue in meat, determines the background tenderness and affects digestibility of meat. Heating may induce great changes in protein structure and its pepsin-treated digestion. The objective of this study was to investigate how heating affected type I collagen structure and in vitro pepsin-treated digestion.

The effect of meat processing methods on changes in disulfide bonding and alteration of protein structures: impact on protein digestion products.

We investigated the effects of different pork preparation methods (cooked pork, emulsion-type sausage, dry cured pork, and stewed pork) on protein structures and digestion. Compared with raw meat, processed meats contained lower levels of free sulfhydryl groups ( < 0.05).