Effect of heat treatment on protein oxidation in pig meat

Traoré, S.; Aubry, Laurent; Gatellier, Philippe; Przybylski, Wiesław; Jaworska, Danuta; Kajak-Siemaszko, Katarzyna; Santé-Lhoutellier, Véronique

doi:10.1016/j.meatsci.2011.11.037

Cited by 126 publications

(108 citation statements)

References 62 publications

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“…As previously observed for free thiol groups, SB formation in chicken charqui seems to be associated with long heating times. Traore et al (2012) also observed a strong increase in SB fluorescence of pig meat after increasing the time of cooking. The high content of SB in grilled and fried samples may also be ascribed to the formation of Maillard fluorescent products, which appears as temperature increases (Silván et al 2006).…”

Section: Schiff Base (Sb) and Disulphide Bond Formationmentioning

confidence: 75%

“…Thermal processing can negatively affect the quality of meat and meat products by increasing reactive oxygen species (ROS) production. In fact, the application of cooking technologies has been associated with thermal denaturation of protein, which induces structural changes that increase protein carbonylation gain in meat products (Traore et al 2012;Estévez 2011). The effect of desalting and cooking methods on the concentration of protein carbonyls (AAS ?…”

Section: Protein Carbonylationmentioning

confidence: 99%

“…2), indicating that protein crosslinking formation and carbonylation of chicken charqui could be associated with the application of high cooking temperature. During heating of meat products, thiol groups are exposed and hydrophobic residues are exteriorized, leading to a breakdown in hydrogen bonds and the formation of disulphide bridges (Traore et al 2012).…”

Section: Schiff Base (Sb) and Disulphide Bond Formationmentioning

confidence: 99%

“…Traore et al (2012) observed increased carbonylation, aggregation and impaired water holding capacity (WHC) in pork subjected to a heat treatment (100°C/30 min) simulating roasting conditions. According to the same authors (Traore et al 2012) the formation of protein carbonyls may alter the ability of proteins to interact chemically with water molecules while aggregation stresses the impaired WHC by restraining the available surface for water binding. Similar oxidative deterioration has been reported to occur in proteins from cooked chicken (Xiao et al 2011) and beef (Gatellier et al 2010).…”

Section: Introductionmentioning

confidence: 99%

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Effect of the cooking method (grilling, roasting, frying and sous-vide) on the oxidation of thiols, tryptophan, alkaline amino acids and protein cross-linking in jerky chicken

et al. 2016

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Broiler breast (pectoralis major) meat was submitted to salting with NaCl ? NaNO 3 followed by a drying process to produce jerky-type chicken. The final product (raw broiler charqui) was desalted and then cooked using grilled, roasted, fried and sous-vide techniques. Sous-vide cooked samples showed lowest results of moisture loss compared to roasted and fried ones. Fatty acid profile suffered minor changes after cooking of broiler charqui. Regarding to protein oxidation, tryptophan fluorescence, protein carbonylation and disulphide bonds formation of chicken charqui were affected by cooking temperature while free thiol groups, Schiff base formation and hardness were mostly impacted by the length of cooking. Instrumental color of broiler charqui was affected by the type of cooking, being closely related with Maillard products formation. In conclusion, sous-vide technique seems to be the most advantageous cooking method to obtain high-quality ready-to-eat chicken charqui.

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Section: Schiff Base (Sb) and Disulphide Bond Formationmentioning

confidence: 75%

Section: Protein Carbonylationmentioning

confidence: 99%

Section: Schiff Base (Sb) and Disulphide Bond Formationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effect of the cooking method (grilling, roasting, frying and sous-vide) on the oxidation of thiols, tryptophan, alkaline amino acids and protein cross-linking in jerky chicken

et al. 2016

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“…3b indicated that heating process reduced fluorescence intensity of HOLA-MP compared with OLA-MP. Heat treatment could enhance the protein cross-linking and aggregation [28], resulting in the decrease of the exposure of tryptophan to the aqueous environment.…”

Section: Tryptophan Fluorescencementioning

confidence: 99%

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

et al. 2016

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Oxidation extent of myofibrillar protein (MP) from silver carp (Hypophthalmichthys molitrix) was affected by the content and type of lipid peroxidation (LPO) products. Oxidized linoleic acid (OLA) was selected as a main representative of lipid peroxidation to investigate the effects of oxidative modification of LPO products on MP structure. Structural changes of the oxidized myofibrillar protein were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. Heating procedure was also applied for further evaluation of gelling properties. The results from SDS-PAGE indicated that aggregation and denaturation of myosin occurred in the oxidized system. The presence of OLA intensified oxidation-initiated loss of a-helix conformation as well as tertiary structure of MP. With the addition of OLA concentration less than 3 mM, a remarkably enhanced gelling capacity of MP was observed. While the excessive covalent bond (OLA > 5 mM) could lead to the breakage of protein-protein bonds, causing the collapse of the gel structure. The gelation procedure induced by OLA involved simultaneous protein oxidation and internal cross-linking.

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Carbon, nitrogen and oxygen isotope fractionation during food cooking: Implications for the interpretation of the fossil human record

Royer

Daux

Fourel

et al. 2017

American J Phys Anthropol

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Reconstructions of paleodietary may thus suffer slight bias in cases of populations with undiversified diets that are restrained toward a specific raw or cooked product, or using a specific cooking mode. In cases of oxygen isotope compositions from skeletal remains (bones, teeth), they not only constitute a valuable proxy for reconstructing past climatic conditions, but they could also be used to improve our knowledge of past human diet.

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Effect of heat treatment on protein oxidation in pig meat

Cited by 126 publications

References 62 publications

Effect of the cooking method (grilling, roasting, frying and sous-vide) on the oxidation of thiols, tryptophan, alkaline amino acids and protein cross-linking in jerky chicken

Effect of the cooking method (grilling, roasting, frying and sous-vide) on the oxidation of thiols, tryptophan, alkaline amino acids and protein cross-linking in jerky chicken

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

Carbon, nitrogen and oxygen isotope fractionation during food cooking: Implications for the interpretation of the fossil human record

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