RESUMEN
Changes in sarcoplasmic and myofibrillar proteins, free amino acids, and cathepsin activities were measured to evaluate the contribution of cathepsins to the proteolysis of muscle proteins in dry-cured duck processing. Thirty-six dry-cured ducks were processed with the traditional method, and samples were collected at different stages. Sarcoplasmic and myofibrillar proteins were found to be degraded to some degree at different stages, whereas content of free amino acids increased from 43.9 to 133.97 mg/100 g during the whole process. Cathepsin B, D, and L activities decreased significantly, and the activities in the end product were 22.4, 26.2, and 40.5% of those in the raw material, respectively. Statistical analysis showed there were significant correlations among changes in proteins, free amino acids, and cathepsin activities. The results indicated that cathepsins are involved in the proteolysis of muscle proteins in dry-cured duck processing.
Asunto(s)
Proteínas Aviares/metabolismo , Conservación de Alimentos , Proteínas Musculares/metabolismo , Péptido Hidrolasas/metabolismo , Productos Avícolas/análisis , Animales , Catepsina B/metabolismo , Catepsina D/metabolismo , Catepsina L/metabolismo , Patos , Electroforesis en Gel de Poliacrilamida/veterinaria , Masculino , Fibras Musculares Esqueléticas/metabolismo , Miofibrillas/metabolismo , ProteolisisRESUMEN
In this study, we investigated the effects of cold atmospheric plasma (CAP) technology on endogenous enzyme characteristics and muscle protein properties of the golden pomfret (Trachinotus ovatus) under different treatment power and time conditions. Results showed that the enzymatic activity of cathepsin B, L, and calpain in crude protease extracts (CPE) decreased significantly as the treatment power and treatment time of CAP increased (p < 0.05). Oxidative degradation of the CPE after exposure to CAP resulted in significant changes in the structure, total sulfhydryl, and carbonyl content of the CPE (p < 0.05). CAP of an appropriate intensity resulted in significant improvements in the color parameters, hydration properties, and textural property parameters of muscle proteins (p < 0.05). These results suggest that CAP, as a non-thermophysical modification technique, can inhibit the activity of endogenous enzymes as well as alter the protein function in food.
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Proteínas Musculares , Gases em Plasma , Animales , Gases em Plasma/farmacología , PecesRESUMEN
The inactivation effects and mechanism of ohmic heating (OH) on Bacillus cereus ATCC 11778 were investigated in this study, conventional heating (CH) was also carried out and served as control. All OH treatments (10 V/cm 50 Hz, 10 V/cm 500 Hz, 5 V/cm 50 Hz and 5 V/cm 500 Hz) could achieve a comparable inactivation effect with CH, while OH treatments significantly shortened the processing time. OH treated cells exhibited significantly higher leakage of metal ions (Mg2+ and K+) and biomacromolecules (nucleic acids and proteins) than those treated with CH when bacterial suspensions were heated to the same temperature. Moreover, OH treatment caused more damage on membrane structure, greatly decreased the cell membrane potential and endogenous enzyme activity than that of CH. The results of this study indicated that OH is more efficient in the inactivation of bacteria.
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Bacillus cereus , Calefacción , Calor , TemperaturaRESUMEN
Coppa Piacentina is considered a peculiar dry cured salami, since it is manufactured by the entire neck muscles stuffed and matured in natural casings, the same as dry cured ham and fermented dry cured sausages. In this work the proteolysis of external and internal portions was investigated by a proteomic approach and by amino acids analysis. Samples of "Coppa Piacentina" were analyzed at 0 days and after 5 and 8 months of ripening through mono- and two-dimensional gel electrophoresis. Image analysis of 2D electrophoretic maps indicated a more intense enzyme activity on the external part, mainly due to endogenous enzymes. They favored, respectively, myofibrillar or sarcoplasmic proteins at 5 or 8 months of ripening. Free amino acids determination proved that lysine and glutamic acid were the most represented ones, followed by a free amino acids sequence like that of dry cured ham. The peculiarities of "Coppa Piacentina" were characterized by a slow proteolysis, due to sacking and binding of the whole cut of the pork neck.
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Productos de la Carne , Proteómica , Proteolisis , Proteínas , AminoácidosRESUMEN
Storage via freezing remains the most effective approach for fish preservation. However, lipid oxidation and protein denaturation still occur during storage, along with nutritional loss. The extent of lipid alteration and protein denaturation are associated with human health defects. To precisely predict common carp (Cyprinus carpio) nutritional quality change during frozen storage, here, we first determined lipid oxidation and hydrolysis and protein denaturation of common carp fillets during 17 weeks of frozen preservation at 261 K, 253 K, and 245 K. Results showed that the content of thiobarbituric acid reactive substances (TBARS) and free fatty acids (FFA) were significantly increased. However, salt-soluble protein (SSP) content, Ca2+-ATPase activity, and total sulfhydryl (SH) content kept decreasing during frozen storage, with SSP content decreasing by 64.82%, 38.14%, and 11.24%, respectively, Ca2+-ATP enzyme activity decreasing to 12.50%, 18.52%, and 28.57% Piµmol/mg/min, and SH values decreasing by 70.71%, 64.92%, and 56.51% at 261 K, 253 K, and 245 K, respectively. The values at 261 K decreased more than that at 253 K and 245 K (p < 0.05). Ca2+-ATPase activity was positively correlated (r = 0.96) with SH content. Afterwards, based on the results of the above chemical experiments, we developed a radial basis function neural network (RBFNN) to predict the modification of lipid and protein of common carp fillets during frozen storage. Results showed that all the relative errors of experimental and predicted values were within ±10%. In summary, the quality of common carp can be well protected at 245 K, and the established RBFNN could effectively predict the quality of the common carp under frozen conditions at 261-245 K.
RESUMEN
Herein, the protective pattern of bilayer film on the texture stability of fillets was discussed in terms of endogenous enzyme activity, as well as protein oxidation and degradation. The texture properties of fillets wrapped with nanoparticles (NPs) bilayer film were greatly improved. NPs film delayed protein oxidation by inhibiting the formation of disulfide bond and carbonyl group as evidenced by the increase of α-helix ratio (43.02%) and the decrease of random coil ratio (15.87%). The protein degradation degree of fillets treated with NPs film was lower than that of control group, specifically with a more regular protein structure. The exudates accelerated the degradation of protein, while NPs film effectively absorbed exudates to delay protein degradation. Overall, the active agents in the film were released into the fillets to play an antioxidant and antibacterial roles, and the inner layer of film could absorb exudates, thus maintaining the texture characteristics of fillets.
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Carpas , Conservación de Alimentos , Animales , Alimentos Marinos/análisis , Proteolisis , Exudados y TransudadosRESUMEN
Impacts of atmospheric cold plasma (ACP) on the properties of muscle protein and performance of extracted crude enzyme of hairtail (Trichiurus Lepturus) fish have been evaluated. A decrease in extracted crude enzyme activity with increasing the ACP treatment time has been found, and the highest reduction (p < 0.05) value of 0.035 units/mg proteins was obtained after 240 s. A considerable increase in the carbonyl content in the treated sample for about three times higher than the control sample was found, and a decrease of total sulfhydryl content to 0.34 nmol/mg protein. Texture profile analysis, water holding capacity, and the color properties of the muscle protein improved significantly in the samples treated with ACP. SDS-PAGE pattern showed an increase in the band intensity of cross-linked myosin heavy chains and actin proteins. Based on these outcomes, ACP could play a significant role as a promising non-thermal method to prolong the shelf-life of hairtail fish.
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Proteínas de Peces/química , Proteínas Musculares/química , Perciformes , Gases em Plasma/química , Animales , Color , Electroforesis en Gel de Poliacrilamida , Enzimas/química , Enzimas/metabolismo , Productos Pesqueros , Proteínas de Peces/metabolismo , Calidad de los Alimentos , Almacenamiento de Alimentos , Congelación , Proteínas Musculares/metabolismo , Carbonilación Proteica , Factores de Tiempo , AguaRESUMEN
The study evaluated the inhibitory effects of chitosan-based coatings on endogenous enzyme activities, proteolytic degradation and texture softening of grass carp (Ctenopharyngodon idellus) fillets stored at 4⯰C for 15â¯days. In general, the inhibitory effects of chitosan coating were worse than that of chitosan composite coatings, which significantly inhibited cathepsin B, Bâ¯+â¯L and calpain activities of fillets, with the most reductions of 58%, 65% and 41%, respectively when compared to the corresponding values of control fillets. Besides, the treatments also retarded the proteolytic degradation through quantifiable indicators including salt-soluble proteins (SSP), TCA-soluble peptides and SDS-PAGE pattern. After storage of 15â¯days, the shear forces of coated fillets were 28-53% higher than that of control samples. These results indicated that chitosan composite coating combined with glycerol monolaurate and clove essential oil improved the quality of refrigerated grass carp fillets by alleviating endogenous enzyme induced proteolysis and softening.