RESUMEN
The Leuconostoc mesenteroides subsp. IMAU:80679 (LM) was chosen for its superior capability in enhancing redness, and was incubated in a broth system containing metmyoglobin (MetMb) to investigate its mechanisms for color improvement. The a* value of LM group reached its highest level of 52.75 ± 1.04 at 24 h, significantly higher than control of 19.75 ± 0.6 (p < 0.05). The addition of LM could inhibit myoglobin oxidation to some extent. Meanwhile, higher content of nitrosylmyoglobin (NOMb) and Zn-protoporphyrin (Znpp) were observed in LM samples during the whole incubation period. Furthermore, enzymatic activity and encoded genes related to MetMb reduction and pigment formation were determined to explain its possible mechanism on color enhancement. Finally, by extracting crude enzymes and adding them to meat batters, the redness of crude enzyme group was comparable to that achieved with 20 ppm nitrite, providing a potential method on compensating for nitrite/nitrate substitution in meat products.
Asunto(s)
Leuconostoc mesenteroides , Mioglobina , Mioglobina/metabolismo , Leuconostoc mesenteroides/genética , Leuconostoc mesenteroides/metabolismo , Nitritos , Carne , Metamioglobina , Oxidación-Reducción , ColorRESUMEN
Colour is one of the important quality traits affecting the meat purchasing decision by consumers, and myoglobin is the principal heme protein responsible for the meat colour. This study aimed to investigate the effects of pH (5.3, 5.8, 6.4 and 7.4) and temperature (4 and 25 °C) on oxymyoglobin (OxyMb) oxidation in model reaction mixtures containing OxyMb, fatty acids (C18:2n-6 and C18:3n-3) and vitamin E. A decrease of the OxyMb concentration with increased acidity was observed for all the reaction mixtures with/without fatty acids and vitamin E. After 48 h of storage at 4 °C, the OxyMb concentration decreased by approximately 60-70%, 61-69%, 53.7-53.9% and 40.93-41.84% in the reaction mixtures containing [OxyMb + C18:2n-6 or C18:3n-3] at pH 5.3, 5.8, 6.4 and 7.4, respectively. While, after 48 h at 25 °C, the OxyMb concentration decreased by 95-98% in all the reaction mixtures containing [OxyMb + C18:2n-6 or C18:3n-3] under all the pH conditions. The presence of vitamin E significantly inhibited the OxyMb oxidation in the reaction mixtures containing fatty acids under acidic conditions, but a higher level of vitamin E may be required for meat(s) containing high n-3 fatty acids content that are stored at high temperature.
RESUMEN
Reactive carbonyl compounds are a large group of highly reactive electrophilic compounds containing one or more carbonyl groups, which can be created by lipid oxidation both in vivo and in food. Malondialdehyde (MDA) and 4-hydroxy-2-nonenel (HNE) are the two most important reactive carbonyl compounds in food. They can react with proteins and nucleic acids and cause biological damage to cells and lead to carbonyl stress. Therefore, they are regarded as representative products of lipid oxidation, toxic molecules, and biomarkers of oxidative stress. Apart from biological toxicity, they can also react with myoglobin and myofibrillar protein and further affect color, gel properties, hydrophobicity, or other properties of food. However, the effects of MDA and HNE on food qualities have not received as much attentions and it is noteworthy that the existing analytical methods for detecting MDA and HNE have a variety of limitations due to the complexity of food samples. To provide a comprehensive understanding of HNE and MDA, the formation mechanism, occurrence, and analytical methods for MDA and HNE in food matrix were summarized in this article. Emphasis is focused on formation mechanism including non-enzymatic pathway and enzymatic pathway, and detection methods including the extraction methods, the new development of sample pre-treatment technology and the selection of derivative reagents. Impressively, the reaction mechanism of MDA and HNE with myoglobin or myofibrillar protein is also described to explain how MDA and HNE affect food quality.
Asunto(s)
Aldehídos/química , Calidad de los Alimentos , Malondialdehído/química , Aldehídos/análisis , Aldehídos/metabolismo , Biomarcadores , Peroxidación de Lípido , Malondialdehído/análisis , Malondialdehído/metabolismo , Proteínas Musculares , Mioglobina , Estrés OxidativoRESUMEN
The effects of low frequency magnetic field on myoglobin (Mb) oxidation stability were evaluated by treatments at 0, 3, 6, 9, 12â¯mT and storage for 10â¯h. The results showed that Mb oxidation was inhibited under all magnetic field treatments, due to the increase of total sulfhydryl and free amino groups (9 or 12â¯mT) from unfolding of Mb clusters (3, 9, 12â¯mT) as well as ß-turn and ß-sheet structures (9 or 12â¯mT). The unfolding also induced (i) the destruction or burial of iron porphyrin and tyrosine residues; (ii) the exposure of tryptophan; (iii) more uniform Mb particle size distribution (3, 9, 12â¯mT) and increased zeta potential (3, 6, 12â¯mT). Overall, magnetic field promoted exposed active groups as the preferred oxidation target, thus decreasing the oxidation rate of central iron atoms. It also promoted Mb stability by redistributing particle size and increasing zeta potential.
Asunto(s)
Mioglobina/química , Aminas/análisis , Campos Magnéticos , Oxidación-Reducción , Tamaño de la Partícula , Conformación Proteica en Lámina beta , Estabilidad Proteica , Desplegamiento Proteico , Compuestos de Sulfhidrilo/análisisRESUMEN
This study aimed to evaluate the effects of l-lysine (Lys)/l-arginine (Arg)/l-cysteine (Cys) on the color of cured sausage and the possible mechanism underlying these effects. The results indicated that the combined addition of Arg/Lys/Cys and NaNO2 effectively increased the a* values and nitroso pigment content but decreased the MetMb(Fe3+) content in cured sausage, compared with the individual addition of Arg/Lys/Cys and NaNO2. The cured sausage treated with combined Arg/Lys/Cys and NaNO2 contained significantly lower residual nitrite than those treated with only NaNO2. UV-vis spectroscopy and electron paramagnetic resonance spectroscopy revealed that pentacoordinate nitrosyl ferrohemochrome was the main pigment component in the cured sausage treated with NaNO2 or combined Arg/Lys/Cys and NaNO2 and higher content in the latter one. The results suggest that Arg/Lys/Cys hindered myoglobin oxidation and promoted pentacoordinate nitrosylmyoglobin formation, which could contribute to the improved color of cured sausage. The results are of interest in the meat industry.
Asunto(s)
Arginina/farmacología , Cisteína/farmacología , Lisina/farmacología , Mioglobina/metabolismo , Carne Roja , Animales , Color , Conservación de Alimentos/métodos , Óxido Nítrico , Oxidación-Reducción , Nitrito de SodioRESUMEN
This work investigated the interrelationship among myoglobin, lipid, and protein oxidations in rabbit meat during refrigerated and superchilled storage. Peroxide value gradually increased (pâ¯<â¯0.05) and decreased thereafter (pâ¯>â¯0.05) with increased storage time for both storage treatments. Thiobarbituric acid-reactive substances (TBARS) significantly increased (pâ¯<â¯0.05) throughout the storage time for the storage temperature considered. The metmyoglobin proportion markedly increased (pâ¯<â¯0.05) and remained constant thereafter (pâ¯>â¯0.05). For both storage temperature levels, the extractable heme iron content significantly declined (pâ¯<â¯0.05), whereas non-heme iron content considerably increased (pâ¯<â¯0.05). With prolonged storage time, the protein carbonyl content significantly increased (pâ¯<â¯0.05), along with significant loss in sulfhydryl content (pâ¯<â¯0.05). Superchilled samples maintained lower rates of increase in metmyoglobin content, TBARS, and protein carbonyl content compared with refrigerated samples. Moreover, principal component analysis presented good correlations between TBARS, protein carbonyls and metmyoglobin content. Taken together, myoglobin, lipid and protein oxidations occurred concurrently in rabbit meat during both storage treatments and each oxidation process seemed to promote the other.
Asunto(s)
Carne/análisis , Mioglobina/análisis , Refrigeración/métodos , Animales , Almacenamiento de Alimentos/métodos , Congelación , Hierro de la Dieta/análisis , Peroxidación de Lípido , Metamioglobina/análisis , Oxidación-Reducción , Carbonilación Proteica , Proteolisis , Conejos , Sustancias Reactivas al Ácido Tiobarbitúrico/análisisRESUMEN
BACKGROUND: Following public concern on the use of synthetic food antioxidants, there is an increasing demand for the application of mixed or purified natural antioxidants to maintain quality of meat products quality during storage. The aim of this research was to investigate the effect of ethanolic extract of hawthorn berry, compared to butylated hydroxylanisole (BHA), on lipid peroxidation, myoglobin oxidation, protein electrophoresis pattern, consistency and firmness of minced pork during refrigeration at 4 °C, and to identify the relationship between chemical modifications and consistency variation. RESULTS: After 6 days of refrigeration it was found that the thiobarbituric acid reactive substances value of minced pork containing 200 mg GAE kg-1 total phenolics in minced meat (200 HP) was significantly lower (0.1543 ± 0.006 mg) compared to BHA-treated meat. The ratio of oxymyoglobin to metmyoglobin in treated minced pork was respectively 0.845 for 200 HP and 0.473 for BHA-treated minced meat. Concentrations of 100 HP or 300 HP will generate statistically higher firmness than BHA in minced pork. CONCLUSION: Hawthorn berry ethanolic extract was more effective than BHA in reducing lipid oxidation and protein degradation, for maintaining firmness and consistency of minced pork during 6 days of refrigeration at 4 °C. © 2017 Society of Chemical Industry.
Asunto(s)
Hidroxianisol Butilado/farmacología , Crataegus/química , Frutas/química , Productos de la Carne/análisis , Extractos Vegetales/farmacología , Porcinos , Animales , Etanol , Conservación de Alimentos/métodos , Peroxidación de Lípido/efectos de los fármacos , Metamioglobina/análisis , Mioglobina/análisis , Mioglobina/química , Mioglobina/efectos de los fármacos , Oxidación-Reducción , Fenoles/farmacología , Refrigeración , Sustancias Reactivas al Ácido Tiobarbitúrico/análisisRESUMEN
Proteomics can be used to characterize quality defects including pale, soft, and exudative (PSE) meat (pork and poultry), woody broiler breast meat, reddish catfish fillets, meat toughness, and beef myoglobin oxidation. PSE broiler meat was characterized by 15 proteins that differed in abundance in comparison to normal broiler breast meat, and eight proteins were differentially expressed in woody breast meat in comparison to normal breast meat. Hemoglobin was the only protein that was differentially expressed between red and normal catfish fillets. However, inducing low oxygen and/or heat stress conditions to catfish fillets did not lead to the production of red fillets. Proteomic data provided information pertaining to the protein differences that exist in meat quality defects. However, these data need to be evaluated in conjunction with information pertaining to genetics, nutrition, environment of the live animal, muscle to meat conversion, meat quality analyses and sensory attributes to understand causality, protein biomarkers, and ultimately how to prevent quality defects.
Asunto(s)
Calidad de los Alimentos , Carne/análisis , Proteómica/métodos , Animales , Bagres , Bovinos , Color , Mioglobina/análisis , Aves de Corral , Proteínas/química , PorcinosRESUMEN
Colour and oxidative stability of minced meat from fresh and frozen/thawed fallow deer was investigated. For the seven fallow deer harvested, half of the meat was minced fresh and half was frozen (-20°C) for 2months under vacuum prior to grinding. Surface colour attributes, myoglobin content and surface redox forms, pH and lipid oxidation of the mince were measured during eight days of display storage. Proximate composition was determined in mince on day 0, fatty acid composition on day 0 and 8. Freezing had no effect on the proximate composition or fatty acid composition of the mince. Frozen meat mince had lower (P≤0.05) total myoglobin content but higher (P≤0.05) decrease in redness (a*) during display storage, higher (P≤0.05) accumulation of metmyoglobin at the surface from day 2 and higher (P≤0.05) TBARS values. Results showed shorter colour and oxidative stability for frozen meat mince as compared to mince from fresh meat. Display storage however did not affect fatty acid composition.
Asunto(s)
Manipulación de Alimentos , Carne Roja/análisis , Animales , Color , Ciervos , Ácidos Grasos/análisis , Embalaje de Alimentos , Congelación , Concentración de Iones de Hidrógeno , Metamioglobina/metabolismo , Músculo Esquelético/química , Oxidación-Reducción , Sustancias Reactivas al Ácido Tiobarbitúrico/análisis , VacioRESUMEN
The influence of animal age and muscle source on the oxidative stability of yak steaks was examined. Longissimus thoracis (LT) muscles from yaks of different age groups (0.5, 1.5, 2.5, and 3.5 years), and three muscle sources of LT, Psoas major (PM), and Biceps femoris (BF) from yaks of 0.5, 1.5, and 2.5 years, were evaluated for metmyoglobin content, activity of antioxidant enzymes, and antioxidant capacity. Oxidative stability was influenced (P<0.05) by muscle source and animal age. LT steaks from 0.5, 1.5, and 2.5 year old yaks exhibited lower (P<0.05) metmyoglobin content than their PM and BF counterparts. Furthermore, LT steaks from 3.5 year old yaks demonstrated lower (P<0.05) metmyoglobin content and greater (P<0.05) activities of antioxidant enzymes than LT steaks from other age groups. These results indicated the necessity to develop muscle- and age-specific processing strategies to improve color and oxidative stability of yak meat.
Asunto(s)
Envejecimiento , Proteínas en la Dieta/análisis , Calidad de los Alimentos , Almacenamiento de Alimentos , Carne/análisis , Proteínas Musculares/análisis , Músculo Esquelético/química , Mataderos , Animales , Antioxidantes/análisis , Antioxidantes/metabolismo , Bovinos , China , Proteínas en la Dieta/química , Masculino , Metamioglobina/análisis , Metamioglobina/química , Metamioglobina/metabolismo , Proteínas Musculares/química , Proteínas Musculares/metabolismo , Músculo Esquelético/crecimiento & desarrollo , Músculo Esquelético/metabolismo , Oxidación-Reducción , Oxidorreductasas/análisis , Oxidorreductasas/química , Oxidorreductasas/metabolismo , Pigmentos Biológicos/análisis , Pigmentos Biológicos/química , Pigmentos Biológicos/metabolismo , Estabilidad Proteica , Refrigeración , Propiedades de SuperficieRESUMEN
Metabolic intermediates of glycolysis and the tricarboxylic cycle can stabilize beef color through improved metmyoglobin-reducing activity. Inorganic redox reactive iron (RRI) forms are pro-oxidants that have been shown to oxidize myoglobin in model systems. This study investigated how RRI, in the presence of added metabolic intermediates lactate and succinate, influences myoglobin (Mb) redox stability and color of beef strip loin homogenates and how it affects mitochondrial respiration. Homogenates with added RRI and either lactate or succinate had lower (p < 0.05) a* values than control homogenates. Oxymyoglobin increased (p < 0.05) as ferrous ion increased in the lactate and succinate treatments. The presence of ferrous or ferric ions reduced the mitochondrial oxidation rates of lactate and succinate (p < 0.05). The benefit of color stability offered by the metabolic intermediates and mitochondria-assisted metmyoglobin reduction was reduced by inorganic iron ions.