Autoxidation Of Myoglobin Research Articles

Maillard reaction products inhibit lipid oxidation by regulating myoglobin stability in washed muscle model.

Lipid oxidation significantly contributes to muscle deterioration, with heme protein oxidation playing a crucial role in this process. This study investigated the inhibition of heme protein oxidation by Maillard reaction products (MRPs) using a washed muscle model combining washed carp with myoglobin (Mb). Protein oxidation products, protein texture, and lipid oxidation levels were assessed. Results showed that metmyoglobin (MetMb) is a primary driver of lipid oxidation in meat, likely due to Mb oxidation, exposing hydrophobic groups that bind to lipids. MRPs at concentrations of 0.5% and 1% effectively inhibited Mb oxidation. Specifically, treatment with 1% MRPs reduced MetMb formation by 15.38%, protein carbonyl content by 6.53%, hydroxyl radical content by 20.37%, protein aggregation by 40.81%, and particle size by 36.95% during later storage stages, thereby preserving Mb stability. In the Mb-mediated oxidation model, 1% MRPs inhibited the formation of primary and secondary oxidative metabolites by 59.47% and 68.19%, respectively, while maintaining muscle tissue texture integrity. PRACTICAL APPLICATION: The antioxidation of Maillard reaction products (MRPs) improves the stability of common carp. By inhibiting the autoxidation of myoglobin and lipid, MRPs help preserve the texture and color of fish muscle while extending its shelf life. This study provides a valuable reference for effectively controlling lipid oxidation in refrigerated fish products and enhancing their overall quality.

Modelling the autoxidation of myoglobin in fresh meat under modified atmosphere packing conditions

Modified atmosphere packing (MAP) is a technique to increase the shelf life of fresh meat. Continuing development of MAP requires better understanding of the physical and chemical processes taking place, in particular the diffusion of oxygen and its reaction with myoglobin. We model these processes using reaction-diffusion equations. The reactions include binding of oxygen to myoglobin, oxidation of myoglobin and other oxygen consuming processes. Model parameters have been extrapolated using data from the literature to relevant temperatures and pH values. Partial agreement with spatially resolved pigment concentration data is obtained, but only by substantially increasing the value of the oxygen consumption rate. Application of the model to meat stored at 5 °C shows that the metmyoglobin layer forms under the surface over a time scale of 24 h; The metmyoglobin layer forms deeper inside the meat proportional to the logarithm of the headspace oxygen partial pressure, thus improving the colour appearance of the meat.

Myoglobin microplate assay to evaluate prevention of protein peroxidation

The current therapeutic strategies are based on the design of multifunctional drug candidates able to interact with various disease related targets. Drugs that have the ability to scavenge reactive oxygen species (ROS), beyond their main therapeutic action, may prevent the oxidative damage of biomolecules. Therefore, analytical approaches that monitor in a continuous mode the ability of drugs to counteract peroxidation of physiologically relevant biotargets are required.In the present work, a microplate spectrophotometric assay is proposed to evaluate the ability of selected cardiovascular drugs, including angiotensin-converting enzyme (ACE) inhibitors, β -blockers and statins to prevent protein peroxidation. Myoglobin, which is a heme protein, and peroxyl radicals generated from thermolysis of 2,2′-azo-bis(2-amidinopropane) dihydrochloride at 37°C, pH 7.4 were selected as protein model and oxidative species, respectively. Myoglobin peroxidation was continuously monitored by the absorbance decrease at 409nm and the ability of drugs to counteract protein oxidation was determined by the calculation of the area under the curve upon the myoglobin oxidation. Fluvastatin (AUC50=12.5±1.2μM) and enalapril (AUC50=15.2±1.8μM) showed high ability to prevent myoglobin peroxidation, providing even better efficiency than endogenous antioxidants such as reduced glutathione. Moreover, labetalol, enalapril and fluvastatin prevent the autoxidation of myoglobin, while glutathione showed a pro-oxidant effect.

Suppressive effect of ATP on autoxidation of tuna oxymyoglobin to metmyoglobin

The discoloration of tuna meat proceeds during frozen storage at around −20 °C. On the other hand, the discoloration of highly fresh tuna meat could effectively be suppressed even if stored at −20 °C. However, the suppressive mechanism of the discoloration is not well understood. Here the effects of ATP on the autoxidation rate and molecular structure of tuna myoglobin are reported. The autoxidation rate of southern bluefin tuna Thunnus maccoyii myoglobin at 25 °C was suppressed in the presence of ATP especially in acidic pH range. Mixing ATP with myoglobin induced a spectral perturbation in the soret region of myoglobin. This spectral perturbation was observed as a function of the ATP concentration. Quenching of myoglobin fluorescence was also caused by ATP, saturating at around 0.5 mM ATP. According to dynamic light-scattering measurements, the molecular weights of tuna Mb changed from 15.5 to 11.3 kDa with ATP and zeta-potential measurements gave also a negative surface charge without ATP and a positive one with ATP, respectively. The above results indicate that ATP-induces changes in the conformational structure of myoglobin. The effects of ATP on myoglobin could thus provide a possible mechanism to regulate the autoxidation of myoglobin.

Relationship between Oxygen Affinity and Autoxidation of Myoglobin

Studies using myoglobins reconstituted with a variety of chemically modified heme cofactors revealed that the oxygen affinity and autoxidation reaction rate of the proteins are highly correlated to each other, both decreasing with decreasing the electron density of the heme iron atom. An Fe(3+)-O(2)(-)-like species has been expected for the Fe(2+)-O(2) bond in the protein, and the electron density of the heme iron atom influences the resonance process between the two forms. A shift of the resonance toward the Fe(2+)-O(2) form results in lowering of the O(2) affinity due to an increase in the O(2) dissociation rate. On the other hand, a shift of the resonance toward the Fe(3+)-O(2)(-)-like species results in acceleration of the autoxidation through increasing H(+) affinity of the bound ligand.

Accelerated Autoxidation of Myoglobin During the Onset of Ischemia

Accelerated Autoxidation of Myoglobin During the Onset of Ischemia

Characterisation of myoglobin from sardine ( Sardinella gibbosa) dark muscle

Myoglobin from the dark muscle of sardine ( Sardinella gibbosa) with the molecular weight of 15.3 kDa was isolated and characterised. The different myoglobin derivatives exhibited varying thermal unfolding characteristics. Deoxymyoglobin showed a single distinct endothermic peak at 74.5 °C, whereas two transition temperatures were noticeable for oxymyoglobin (64.5 and 78.4 °C) and metmyoglobin (59.0 and 76.0 °C). The spectrum of deoxymyoglobin and oxymyoglobin had absorption bands at 739, 630, 575, 500 and 405 nm, while the disappearance of the peak at 575 nm was found in the spectrum of metmyoglobin. The soret peak of all derivatives was noticeable at 405 nm. The autoxidation of myoglobin became greater at very acidic or alkaline conditions as evidenced by the formation of metmyoglobin, the changes in tryptophan fluorescence intensity as well as the disappearance of soret absorption. The higher temperature, particularly above 40 °C, and the longer incubation time induced the higher metmyoglobin formation as well as the conformational changes.

Pyruvate but not lactate prevents NADH-induced myoglobin oxidation

In this work, we investigated the influence of NADH on the redox state of myoglobin and the roles of pyruvate and lactate in this process. NADH increased the autoxidation rate of myoglobin. Both a drop in pH and partial deoxygenation markedly stimulated the autoxidation process and the influence of NADH. A correlation between met-Mb formation rate and NADH oxidation rate was always observed. The increased rate of Mb autoxidation caused by NADH was inhibited by catalase and pyruvate but not by l-lactate. The antioxidant activity versus H 2O 2 of both pyruvate and lactate was evidenced by chemiluminescence experiments. The antioxidant activity of lactate disappeared completely in the presence of myoglobin or apo-myoglobin, whereas it was only reduced for pyruvate. These results could be of interest in preventing autoxidation of myoglobin that can contribute to ischemia–reperfusion injury during infarction or high–intensity exercise.

Oxymyoglobin oxidation and membrane lipid peroxidation initiated by iron redox cycle: prevention of oxidation by enzymic and nonenzymic antioxidants.

The red color of muscle is principally due to the presence of oxymyoglobin. Oxidation of heme iron from the ferrous to the ferric state produces a brownish color, which consumers find undesirable. The aim of this study was to use enzymic and nonenzymic antioxidants to simulate in situ muscle antioxidation reactions in order to understand better the mechanism by which the iron redox cycle catalyzes membrane lipid peroxidation and oxymyoglobin oxidation. The inclusion of superoxide dismutase (SOD) in the model system decreased oxymyoglobin oxidation by 10% without affecting lipid peroxidation. Addition of catalase decreased oxymyoglobin oxidation by approximately 40% but not lipid peroxidation. Increasing the ceruloplasmin concentration inhibited lipid peroxidation but increased oxymyoglobin oxidation, which was inhibited by SOD and catalase. Conalbumin (50 microM), a specific iron chelator, inhibited peroxidation and oxymyoglobin oxidation by almost 50%. The addition of the antioxidant catechin (500 microM) decreased lipid peroxidation by 90% but oxymyoglobin oxidation by only 50%. Feeding turkeys with vitamin E at several levels significantly increased the alpha-tocopherol level of membranes, thus preventing oxymyoglobin and lipid oxidation. In conclusion, oxymyoglobin stability in the model system was affected by two pathways: (a) oxygen active species, such as O(2)*(-), H(2)O(2), HO*, and ferryl, generated during autoxidation of myoglobin and oxidation of ferrous ions and ascorbic acid; and (b) lipid radicals, such as ROO*, RO*, and hydroperoxides, generated during lipid peroxidation. Maximum inhibition could be achieved only by introducing inhibitors of both pathways into the system.

Relationship between the stability and autoxidation of myoglobin

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRelationship between the stability and autoxidation of myoglobinChau Jen ChowCite this: J. Agric. Food Chem. 1991, 39, 1, 22–26Publication Date (Print):January 1, 1991Publication History Published online1 May 2002Published inissue 1 January 1991https://doi.org/10.1021/jf00001a004RIGHTS & PERMISSIONSArticle Views240Altmetric-Citations31LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (1 MB) Get e-Alerts Get e-Alerts

Reduced stability and accelerated autoxidation of tuna myoglobin in association with freezing and thawing

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTReduced stability and accelerated autoxidation of tuna myoglobin in association with freezing and thawingChau Jen Chow, Yoshihiro Ochiai, Shugo Watabe, and Kanehisa HashimotoCite this: J. Agric. Food Chem. 1989, 37, 5, 1391–1395Publication Date (Print):September 1, 1989Publication History Published online1 May 2002Published inissue 1 September 1989https://doi.org/10.1021/jf00089a040RIGHTS & PERMISSIONSArticle Views109Altmetric-Citations25LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (661 KB) Get e-Alerts Get e-Alerts

Kinetic analysis of myoglobin autoxidation by isoelectric-focusing electrophoresis.

The autoxidation of horse myoglobin was studied in the presence or absence of catalase (EC 1.11.1.6) and/or superoxide dismutase (EC 1.15.1.1) at various pH values (6.6-7.8). Changes in the percentages of oxymyoglobin and metmyoglobin during the reaction were analysed by means of isoelectric focusing on Ampholine gel plates. Oxymyoglobin was decreased in a first-order manner, with an accompanying increase in metmyoglobin, under the various conditions studied. The observed reaction rate constants obtained under these conditions were pH-dependent; however, they were also greatly affected by the presence of the enzymes. The pH-dependence of the overall reaction was explained by the acid-base three-state model of myoglobin proposed by Shikama & Sugawara [(1978) Eur. J. Biochem. 91, 407-413]. The reaction process of myoglobin autoxidation was explained by the model suggested by Winterbourn, McGrath & Carrell [(1976) Biochem. J. 155, 493-502], indicating that superoxide anion and hydrogen peroxide are involved in the reaction mechanism.

Heme dissociation and autoxidation of myoglobin

Heme dissociation and autoxidation of myoglobin

ミオグロビンの自動酸化時における酸素吸収量

To know the amount of oxygen absorbed in the autoxidation of myoglobin (Mb) to metmyoglobin (MMb) is needed for elucidating the mechanism of, and devising the prevention of, fish meat discoloration during freezing storage. So, experiments were carried out to confirm whether or not the oxygen absorption of 2.5±0.3 moles per mole of horse Mb1) is also true for fish Mb's. Crystalline MMb's of two species of tuna, whale, and horse, were dissolved in 0.1M phosphate buffer, pH 6.7, added with small amounts of sodium hydrosulfite, and shaken in air to oxidize excess hydrosulfite. The oxymyoglobin (MbO2) solution thus obtained was subjected to manometric analysis at 30°C using a WARBURG apparatus. The amount of MMb formed during the manometry was estimated by the authors' method5). According to the results, the amount of oxygen absorbed per mole of MMb formed roughly resembled to that reported by GEORGE et al., varying widely as pointed out by them (Table 1). The low reproducibility was assumed to be attributable to the presence of substances interfering in manometry such as decomposition products of hydrosulfite which are able to absorb oxygen, although not to reduce MMb. This assumption was just supported by an experiment on sodium bisulfite, one of such decomposition products (Fig. 1). Therefore, the subsequent experiments were performed on MbO2 solutions, from which the decomposition products of hydrosulfite were previously removed by dialysis before manometry. Thus the absorption amount of oxygen was found to be only about 0.34 mole per mole of Mb, irrespective of the species exam ?? ned, and the results were fairly reproducible (Table 2). And some model experiments were performed to clear up whether large amounts of oxygen are absorbed or not by globin moiety of Mb in the autoxidation, as suggested by GEORGE et at.1) None of several amino acids tested absorbed oxygen in appreciable amounts (Fig. 2). In addition, it was also proved that free sulfhydryl groups were not oxidized during manometric experiments in the case of tuna (Table 3). These results seem to indicate slight, if any, involvement of protein moiety in Mb autoxidation.