BACKGROUND Protein oxidation during food processing causes changes in the balance of protein–molecular interactions and protein–water interactions, ultimately leading to protein denaturation, which results in the loss of a range of functional properties. Therefore, how to control the oxidative modification of proteins during processing has been the focus of research. RESULTS In the present study, the intrinsic fluorescence value of the myofibrillar proteins (MP) decreased and the surface hydrophobicity value increased, indicating that the heat treatment caused a significant change in the conformation of the MP. With an increase in heating temperature, protein carbonyl content increased, total sulfhydryl content decreased, and protein secondary structure changed from α‐helix to β‐sheet, indicating that protein oxidation and aggregation occurred. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis revealed that heat treatment can lead to the degradation of proteins, especially myosin heavy chain, although actin had a certain thermal stability. In total, 733 proteins were identified by proteomics, and the protein oxidation caused by low temperature vacuum heating (LTVH) was determined to be mild oxidation dominated by malondialdehyde and 4‐hydroxynonenal by oxidation site division. CONCLUSION The present study has revealed the effect of LTVH treatment on the protein oxidation modification behavior of sturgeon meat, and explored the effect mechanism of LTVH treatment on the processing quality of sturgeon meat from the perspective of protein oxidation. The results may provide a theoretical basis for the precise processing of aquatic products. © 2023 Society of Chemical Industry.
As an anaerobic butyrate-producing bacterium, Clostridium cellulovorans can secrete a variety of extracellular enzymes to degrade plant-based cellulose. However, with glucose as the carbon source, it still secretes a large amount of protein in the broth. The metabolism and regulation are obscure and need to be further studied. Hence, in this study, C. cellulovorans was used to conduct fed-batch fermentation of glucose and microcrystalline at pH 7.0 to produce a higher level of butyrate in the bioreactor. It produced 16.8 mM lactate, 22.3 mM acetate, and 132.7 mM butyrate in 72 h during glucose fermentation. In contrast, it produced only 11.5 mM acetate and 93.9 mM butyrate and took 192 h to complete the fermentation with cellulose as the carbon source. Furthermore, there was no lactate detected in the broth. The analysis of carbon source balance and redox balance showed that 57% of the glucose was consumed to form acids in glucose fermentation, while only 47% of the cellulose was used for acid generation in the cellulose fermentation. Meanwhile, a large amount of protein was detected in the fermentation broth in both glucose (0.9 ± 0.1 g/L) and cellulose (1.1 ± 0.2 g/L) fermentation. These results showed that protein was also a main product. C. cellulovorans metabolized glucose to generate intermediate metabolites and reducing powers (NADH and Fdred), then protein and acid synthesis consumed this reducing power to maintain the carbon source balance and redox balance in the cell metabolism. The results of comparative transcriptomics and comparative proteomics also supported the above conclusion. The method of studying the protein during Clostridium species fermentation provides a new perspective for further study on metabolic regulation.
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