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This study aimed to investigate the influence of Astragalus membranaceus (AM), Adenophora triphylla (AT), and Ulmus pumila (UP) extracts on the quality traits, palatability, and storage stability of sous-vide (SV) cooked chicken breasts. Chicken breasts were marinated in AM, AT, or UP extracts for 1 h, and then consistently cooked at a constant temperature of 60°C for 2 h. SV cooked chicken breasts with the UP extract exhibited lower lightness and higher yellowness values on the surface region compared to those with the AM and AT extracts (p0.05). Owing to these results regarding overall sensory acceptability, samples from the UP group were more preferred by the trained panelists compared to samples from the control group (p less then 0.001). On 14 d of cold storage, all the groups with herbal medicinal extracts exhibited a lower concentration of thiobarbituric acid-reactive substances than the control group (p less then 0.05), and the AT and UP groups showed lower values compared to the AM group due to their higher flavonoid contents (p less then 0.001). Therefore, meat marination with herbal plant extracts before SV cooking can be effective for enhancing the overall quality of SV cooked chicken breast.The objective of this study was to examine the relationship between meat quality attributes and the changes of sarcoplasmic protein acetylation and myofibrillar protein acetylation in lamb longissimus thoracis et lumborum muscles at different postmortem phases. Protein acetylation, color, pH, shear force, myofibril fragmentation index and cooking loss were measured. The total level of acetylated sarcoplasmic proteins showed a negative relation with pH, a positive relation with a*, b* and cooking loss at the pre-rigor phase. Sarcoplasmic proteins acetylation affected postmortem pH by regulating glycolysis, which in turn affects color and cooking loss. The total level of acetylated myofibrillar proteins showed a positive relation with shear force at the pre-rigor phase. Myofibrillar proteins acetylation affected meat tenderness by regulating muscle contraction. This study indicated that acetylation played a regulatory role of meat color, water-holding capacity, and tenderization process at early postmortem.The aim of this study was to evaluate the effect of three different strains of lactic acid bacteria (LAB) starter cultures Pediococcus pentosaceus (KC-13100) (PP), Lactobacillus plantarum (KCTC-21004) (LP1), and L. plantarum (KCTC-13093) (LP2) on the physicochemical and microbiological characteristics, and sensory quality of dry fermented sausages after 21 days of drying and ripening period. Treatments added with PP and LP2 strains showed a significant higher (pPP). In sensory attributes, PP treated samples had significantly higher (p less then 0.05) color and overall acceptability scores. The current findings proved how important the optimal assortment of starter culture. Inoculation with PP produced importantly beneficial effects on sensory quality improvement of dry fermented sausage.The effect of deer antler extract on muscle differentiation and muscle atrophy were evaluated to minimize muscle loss following aging. Various deer antler extracts (HWE, hot water extract of deer antler; FE, HWE of fermented deer antler; ET, enzyme-assisted extract of deer antler; UE, extract prepared by ultrasonication of deer antler) were evaluated for their effect on muscle differentiation and inhibition of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR)-induced muscle atrophy in C2C12 cells. Morphological changes according to the effect of antler extracts on muscle differentiation were confirmed by Jenner-Giemsa staining. In addition, the expression levels of genes related to muscle differentiation and atrophy were confirmed through qRT-PCR. https://www.selleckchem.com/autophagy.html In the presence of antler extracts, the length and thickness of myotubes and myogenin differentiation 1 (MyoD1) and myogenic factor 5 (Myf5) gene expression were increased compared to those in the control group (CON). Gene expression of AMP-activated protein kinase (AMPK), MyoD1, and myogenin, along with the muscle atrophy factors muscle RING finger-1 (MuRF-1) and forkhead box O3a (FoxO3a) upon addition of deer antler extracts to muscle-atrophied C2C12 cells was determined by qRT-PCR after treatment with AICAR. The expression of MuRF-1 and FoxO3a decreased in the groups treated with antler extracts compared to that in the group treated with AICAR alone. In addition, gene expression of MyoD1 and myogenin in the muscle atrophy cell model was significantly increased compared that into the CON. Therefore, our findings indicate that antler extract can increase the expression of MyoD1, Myf5 and myogenin, inhibit muscle atrophy, and promote muscle differentiation.Bioactive peptides have great potentials as nutraceutical and pharmaceutical agents that can improve human health. The objectives of this research were to produce functional peptides from ovotransferrin, a major egg white protein, using single enzyme treatments, and to analyze the properties of the hydrolysates produced. Lyophilized ovotransferrin was dissolved in distilled water at 20 mg/mL, treated with protease, elastase, papain, trypsin, or α-chymotrypsin at 1% (w/v) level of substrate, and incubated for 0-24 h at the optimal temperature of each enzyme (protease 55°C, papain 37°C, elastase 25°C, trypsin 37°C, α-chymotrypsin 37°C). The hydrolysates were tested for antioxidant, metal-chelating, and antimicrobial activities. Protease, papain, trypsin, and α-chymotrypsin hydrolyzed ovotransferrin relatively well after 3 h of incubation, but it took 24 h with elastase to reach a similar degree of hydrolysis. The hydrolysates obtained after 3 h of incubation with protease, papain, trypsin, α-chymotrypsin, and after 24 h with elastase were selected as the best products to analyze their functional properties. None of the hydrolysates exhibited antioxidant properties in the oil emulsion nor antimicrobial property at 20 mg/mL concentration. However, ovotransferrin with α-chymotrypsin and with elastase had higher Fe3+-chelating activities (1.06±0.88%, 1.25±0.24%) than the native ovotransferrin (0.46±0.60%). Overall, the results indicated that the single-enzyme treatments of ovotransferrin were not effective to produce peptides with antioxidant, antimicrobial, or Fe3+-chelating activity. Further research on the effects of enzyme combinations may be needed.
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