Myofibrillar proteins primarily consist of myosin, actin, myogenin, and actomyosin. These proteins form complex networks within muscle fibers and are crucial to the physical and chemical properties of meat. Additionally, myofibrillar proteins serve as significant substrates for the adsorption of volatile flavor compounds, including aldehydes, alcohols, ketones, and sulfur and nitrogen compounds, which contribute to the overall flavor profile of meat products. A series of chemical reactions occur during the processing, storage, and transportation of meat products. Oxidation is one of the most significant reactions. Oxidative modification can alter the physical and chemical properties of proteins, ultimately impacting the sensory quality of meat products, including flavor, taste, and color. In recent years, considerable attention has been focused on the effects of protein oxidation on meat quality and its regulation. This study investigates the impact of myofibrillar protein oxidation on the sensory attributes of meat products by analyzing the oxidation processes and the factors that initiate myofibrillar protein oxidation. Additionally, it explores the control of myofibrillar protein oxidation and its implications on the sensory properties of meat products, providing theoretical insights relevant to meat processing methods and quality control procedures.

This study aims to investigate the flavor changes of industrial stir‐frying mutton sao zi, a mutton product popular in the northwest of China, at different stir‐frying stages. Electronic nose (E‐nose) was used to recognize mutton sao zi odors at different processing time points, and the individual volatile compounds were further identified by the solid‐phase microextraction (SPME) combined with gas chromatography–mass spectrometry (GC‐MS). A total of 105 volatile compounds were detected by GC‐MS, of which 51 were major volatile compounds. Additionally, GC‐MS and E‐nose data of the samples were also correlated with the fatty acids, crude composition (moisture, fat, protein), and amino acids. The stir‐frying time and temperature may be the critical contributors to different flavors of industrial stir‐frying mutton sao zi. The signal intensities of W1S, W1W, W2S, W2W, and W3S sensors positively correlate with protein, fat, and 18 amino acids, but negatively with SFA and moisture. Hence, this study explored the flavor changes of industrial stir‐frying mutton sao zi by E‐nose and SPME‐GC‐MS for the first time, providing an insight into the industrial production and flavor control stir‐frying machine of stir‐frying mutton products with household flavor.

Tan lamb is highly recommended breed in China. It is of great significance to understand the underlying mechanism of how water‐soluble flavor precursors metabolize in Tan lamb muscles during the postmortem aging period. In this study, we investigated the muscle pH, lactate dehydrogenase (LDH) activity, and the variations in water‐soluble flavor‐related metabolites. The proteome changes were profiled to provide insights into the biochemical changes affecting accumulation of water‐soluble flavor precursors in different aging stages (days 0, 4, and 8). The results indicated that pH value considerably decreased from day 0 to day 4, and increased from day 4 to day 8 (p < .05). The activity of LDH significantly increased from day 0 to day 4, and decreased from day 4 to day 8 (p < .05). Postmortem glycolysis was activated in 4 days, which directly affected the variations in metabolic enzymes and triggered the accumulation of flavor‐related carbohydrates. The free amino acids accumulated due to hydrolysis of structural proteins, with 3‐hydroxy‐L‐proline, aspartic acid, and methionine increasing from day 0 to day 4, and aspartic acid, serine, threonine, tyrosine, phenylalanine, and D‐phenylalanine from day 4 to day 8. The inosine and hypoxanthine accumulated due to the degradation of ATP. The results of the present study provide insightful information, revealing the differences in biochemical attributes in Tan lamb muscles caused by postmortem aging.