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

Abstract

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 (p < 0.05). The results of tryptophan fluorescence verified that the tertiary structure of the protein seemed to be unfolded at 70 °C. Higher protein denaturation after overheating, as proven by the sulfhydryl contents and turbidity, caused irregular aggregate generation. The excessive heating mode of treatment at 100 °C for 30 min caused myosin to exhibit a lower degree of pepsin digestion, which increased the Michaelis constant (Km value) of pepsin during the digestion, but induced the production of new peptides with longer peptide sequences. This study elucidates the effects of cooking temperature on the conformation of myosin and the change in digestibility of pepsin treatment during heating.

Innovative Implementation of Computational Fluid Dynamics in Proteins Denaturation Process Prediction in Goose Breast Meat and Heat Treatment Processes Optimization

“…Additionally, the intense transverse shrinkage observed in the masseter at 60-70 °C coincided with the later onset of myosin denaturation in this muscle [43]. The study conducted by Zhang et al [44] delves into the intricate effects of thermal processing on the conformational and digestive properties of myosin, a crucial protein in meat. The findings reveal that increasing heating temperatures lead to notable changes in the structural integrity of myosin.…”

“…In contrast, overheating at 100 °C results in a decrease in pepsin sensitivity, as indicated by an increase in the Michaelis constant (Km value) during digestion. However, overheating also prompts the production of new peptides with longer sequences, possibly due to the formation of irregular myosin aggregates [44].…”

Study on the interaction and gel properties of pork myofibrillar protein with konjac polysaccharides

“…The α ‐helix structure is predominantly sustained by the hydrogen bonds among carbonyl oxygen (CO) and amino hydrogen (NH) on the polypeptide chains 8 . And the stability of the hydrogen bonds that helps to maintain the protein structure can be affected by the loss or disruption of the α ‐helix structure, so the increase of α ‐helix content with increasing konjac polysaccharide addition was also in favor of stabilizing the MP structure 35 . According to the view of Fei et al ., 36 there is a positive correlation between natural α ‐helix structure and the WHC of the gel, and thus the preservation of the natural α ‐helix structure is an essential element in the enhancement of the composite gels' WHC.…”

Chemical Compositions and Characteristics of Biocalcium from Pre-Cooked Tuna Bone as Influenced by Sodium Chloride Pretreatment and Defatting by Asian Seabass Lipase

“…Typically, bones are composed of hydroxyapatite, which is localized between gap zones of collagen fibrils [19]. Upon heating, the protein is solubilized, known as thermal solubilization [20]. It is worth noting that the liberation of peptides or proteins, particularly collagen, from the bone matrix led to the rise of the amount of HYP in the pretreatment solutions.…”