The objective of the study was to research the effect of protein oxidation on the biochemical properties of Coregonus peled muscle proteins. Myofibrillar proteins (MP) prepared from C. peled back muscle was oxidized using a hydroxyl radical‐generating system (HRGS: 0.1 mM FeCl3, 0.1 mM ascorbic acid (Asc) and 1–20 mM H2O2). In the HRGS oxidizing system, the carbonyls, dityrosine content, and the surface hydrophobicity of C. peled MP (p < 0.05) increased with the increasing of H2O2 concentration and oxidation time, while the total sulfhydryl, free amino groups and the Ca‐ATPase activity decreased (p < 0.05). The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) pattern reflected the formation of protein polymers and protein degradation. The results indicate that protein oxidation and the increasing levels of biochemical alterations of C. peled MP have influence on the quality of C. peled muscle protein. Practical applications Protein oxidation plays a major role in the meat quality deterioration of C. peled, which always leads to a change in protein physical and chemical properties. In this study, the biochemical change of MP isolates as affected by HRGS oxidation system was proposed. Such chemical modification leads to loss of protein amino groups, shift in the isoelectric point of the protein, loss of solubility and functionality. Additionally, protein carbonyls have been found to be potentially toxic to humans, and relevant measurement of dityrosine as those have been found to cause health problems after oral administration. So such modifications are of technological and nutritional relevance.

The human EGFR family consists of four type-1 transmembrane tyrosine kinase receptors: HER1 (EGFR, ErbB1), HER2 (Neu, ErbB2), HER3 (ErbB3), and HER4 (ErbB4). HER3 can dimerize with EGFR, HER2 and even c-Met and likely plays a central role in the response to EGFR-targeted therapy. Because HER3 lacks significant kinase activity and cannot be inhibited by tyrosine kinase inhibitors, neutralizing antibodies and alternative inhibitors of HER3 have been sought as cancer therapeutics. Here, we describe the stable suppression of HER3 mRNA and protein using siRNA. The inhibition of HER3 expression decreased cell proliferation, suppressed cell cycle progression, induced apoptosis and inhibited cell motility, migration, invasiveness, and soft agar growth. In addition, we found that gefitinib treatment increased the HER3 and HER2 mRNA levels. The administration of various concentrations of gefitinib to HER3-knockdown cells enhanced antitumour activity and sensitivity due to the downregulation of protein phosphorylation via PI3K/AKT and ERK signalling. Our results support the use of combined treatments targeting multiple EGFR receptors, particularly the use of HER3 inhibitors combined with EGFR inhibitors, such as gefitinib.

The aim of this study was to evaluate the effect of µ‐calpain oxidation on Coregonus peled myofibrillar protein degradation. In the present study, a hydroxyl radical oxidation system was selected to investigate oxidative modification on µ‐calpain activity and its degradation on C. peled myofibrillar protein. When subjected to oxidation, the carbonyl content of µ‐calpain significantly increased with the increasing of oxidation levels, and oxidation modification promoted the µ‐calpain activity. Incubation of C. peled myofibrillar protein with oxidized µ‐calpain resulted in the enhanced degradation of myosin heavy chains, actin, and troponin T, but the degradation of desmin at higher levels of oxidation was slightly inhibited, based on sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting. This study suggests that oxidation treatment of µ‐calpain could accelerate myofibrillar proteolysis through regulating the enzyme activity during postmortem aging. Practical Application Endogenous proteases, especially µ‐calpain, are reported to be involved in fish softening during early postmortem storage, which is critical to muscle quality. The cysteine residues of proteins are particularly sensitive to oxidation. The investigation of the effect of oxidation on µ‐calpain (a cysteine protease) activity allows for the monitoring of its role in the postmortem proteolysis of fish myofibrils and the associated softening of fish meat, in an attempt to minimize this softening.

Commercial production of acarbose is exclusively via done microbial fermentation with strains from the genera of Actinoplanes. The addition of C7N-aminocyclitols for enhanced production of acarbose and concurrently reduced formation of impurity C by cultivation of A. utahensis ZJB-08196 in 500-mL shake flasks was investigated, and validamine was found to be the most effective strategy. Under the optimal conditions of validamine addition, acarbose titer was increased from 3560 ± 128 mg/L to 4950 ± 156 mg/L, and impurity C concentration was concurrently decreased from 289 ± 24 mg/L to 107 ± 29 mg/L in batch fermentation after 168 h of cultivation. A further fed-batch experiment coupled with the addition of validamine (20 mg/L) in the fermentation medium prior to inoculation was designed to enhance the production of acarbose. When twice feedings of a mixture of 6 g/L glucose, 14 g/L maltose, and 9 g/L soybean flour were performed at 72 h and 96 h, acarbose titer reached 6606 ± 103 mg/L and impurity C concentration was only 212 ± 12 mg/L at 168 h of cultivation. Acarbose titer and proportion of acarbose/impurity C increased by 85.6% and 152.9% when compared with control experiments. This work demonstrates for the first time that validamine addition is a simple and effective strategy for increasing acarbose production and reducing impurity C formation.