Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins

Morzel, Martine; Gatellier, Philippe; Sayd, Thierry; Renerre, Michel; Laville, Élisabeth

doi:10.1016/j.meatsci.2006.02.005

Cited by 251 publications

(177 citation statements)

References 39 publications

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“…Myofibrillar protein showed higher rate of hydrolysis when treated with thermolysin than of proteinase K. The myofibrillar structure is a complex system with many proteinprotein interactions (Morzel et al 2006) and even proteinlipid interactions (Chelh et al 2007) which can affect its susceptibility to proteolysis (Morzel et al 2006). Solubility of a protein is primarily dependent on the distribution of hydrophobic and hydrophilic amino acids on the surface of a protein and on the thermodynamics of the protein-water interactions (Kristinsson and Rasco 2000).…”

Section: Sds-page Analysismentioning

confidence: 99%

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

et al. 2011

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This study was conducted to evaluate the kinetic characteristics of proteolytic activity of proteases on Channa striatus protein fractions. Degree of hydrolysis (DH), amino acid composition and kinetic parameters of sarcoplasmic and myofibrillar proteins were investigated when incubated with proteinase K and thermolysin, separately. After 30 min incubation with proteases, a decrease in DH of sarcoplasmic protein was observed whereas, hydrolysis of myofibrillar protein with proteases took 2 h with an increase in DH. The major amino acids were glutamic acid (16.6%) in thermolysin-myofibrillar hydrolysate followed by aspartic acid (11.1%) in sarcoplasmic protein fraction with no enzyme treatment and lysine (10%) in thermolysinmyofibrillar hydrolysate. The apparent Michaelis constant of proteinase K was lower than thermolysin for both sarcoplasmic and myofibrillar proteins. However, rate of turnover and enzyme efficiency suggested that sarcoplasmic and myofibrillar proteins are suitable substrates for proteinase K and thermolysin hydrolytic reaction, respectively.

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Section: Sds-page Analysismentioning

confidence: 99%

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

et al. 2011

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“…The nutritional importance of the interaction of proteins with oxidized lipids generally refers to the reduction of the content or availability of essential amino acids and the reduction of a protein digestibility (loss of enzyme activity, protein cross-linking) [Morzel et al, 2006;Santé-Lhoutellier et al, 2008]. Protein-lipid interactions signifi cantly affect the functional properties of proteins, and thus the quality of the product, which usually deteriorates.…”

Section: Introductionmentioning

confidence: 99%

Protein-Lipid Interactions in Different Meat Systems in the Presence of Natural Antioxidants – a Review

Hęś¹

2017

Pol. J. Food Nutr. Sci.

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This study presents several aspects of the mutual interaction between lipids and proteins. Nutritional and technological implications of the reaction of oxidized lipids with proteins are discussed. Changes are highlighted in the content of amino acids and protein digestibility, formation of cross--links, fl avor compounds, as well as the formation of colored non-enzymatic browning products. Attention is paid to the agents which may determine the reaction of amino acids with the products of lipid oxidation, i.e. the presence of catalysts or inhibitors in the environment, the presence of water, pH of the environment, temperature or reaction time. It was also noted that the conformation of the protein structure, the surface charge, the affi nity, and the accessibility of reactive groups affect the intensity of these interactions. This review article presents methods which reduce oxidative rancidity due to the use of antioxidant compounds, particularly the possibility of the use of natural antioxidants that reduce the number of lipid and protein oxidation products, and are simultaneously able to model the nutritional value of food.

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“…Oxidation of proteins can also induce protein polymerisation and aggregation, and thus, change their digestibility and affect the nutritional value of Means (n = 6) indicated with different lowercase letters in the same line (addition effect) and uppercase letters in the same column (storage time effect) are signifi cantly different (oneway ANOVA, Turkey test, P = 0.05). www.food.actapol.net/ meat products [Morzel et al 2006]. Protein oxidation can change the inter-and intermolecular interactions within protein and infl uence its conformation.…”

Section: Eff Ect On Nutritive Valuementioning

confidence: 99%

Effect of ethanolic fl ax (Linum usitatissimum L.) extracts on lipid oxidation and changes in nutritive value of frozen-stored meat products

Waszkowiak¹,

Szymandera‐Buszka²,

Hęś³

2014

Acta Sci Pol Technol Aliment

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Background. Flaxseed (Linum usitatissimum L.) is an important source of phenolic compounds, mainly lignans. Antioxidant capacities of fl axseed extracts that contain the compounds have been reported earlier. However, there is a lack of accessible information about their activity against lipid oxidation in meat products. Therefore, the effect of ethanolic fl axseed extracts (EFEs) on lipid stability and changes in nutritive value of frozen-stored meat products (pork meatballs and burgers) was determined. Material and methods. EFEs from three Polish fl ax varieties (Szafi r, Oliwin, Jantarol) were applied in the study. During 150-day storage of meat products, the lipid oxidation (peroxide and TBARS value) and thiamine retention were periodically monitored, alongside with methionine and lysine availability and protein digestibility.Results. The addition of EFEs signifi cantly limited lipid oxidation in stored meatballs and burgers. EFE from brown seeds of Szafi r var. was superior to the others from golden seeds of Jantarol and Oliwin. Moreover, the extracts reduced changes in thiamine and available lysine content, as well as protein digestibility, during storage time. The effect of EFE addition on available methionine retention was limited. Conclusion. The ethanolic fl axseed extracts exhibit antioxidant activity during frozen storage of meat products. They can be utilized to prolong shelf-life of the products by protecting them against lipid oxidation and deterioration of their nutritional quality. However, antioxidant effi ciency of the extracts seems to depend on chemical composition of raw material (fl ax variety). Further investigations should be carried on to explain the issue.

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Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins

Cited by 251 publications

References 39 publications

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

Protein-Lipid Interactions in Different Meat Systems in the Presence of Natural Antioxidants – a Review

Effect of ethanolic fl ax (Linum usitatissimum L.) extracts on lipid oxidation and changes in nutritive value of frozen-stored meat products

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