Antioxidant enzyme activities in beef in relation to oxidation of lipid and myoglobin

Renerre, Michel; Dumont, Françoise; Gatellier, Ph.

doi:10.1016/0309-1740(96)84583-9

Cited by 165 publications

(141 citation statements)

References 30 publications

Supporting

Mentioning

103

Contrasting

Unclassified

Order By: Relevance

“…In the oxidative muscles of muscles (Daun et al, 2001), which indicated stability chicken, duck, lamb and turkey, GSH-Px activities of GSH-Px. However, our results were different from were significantly higher than those of the glycolytic those on turkey Renerre et al, 1999. muscles (Daun and Akesson, 2004).…”

Section: Determination Of Peroxide Valuecontrasting

confidence: 96%

“…The higher activity of the antioxidant activities of antioxidative enzymes than glycolytic enzymes could lead to a significant increase of muscles such as catalase and GSH-Px (DeVore and resistance to lipid oxidation during meat storage. Such Greene, 1982; Lee et al, 1997;Renerre et al, 1996). was the case in our study.…”

Section: Determination Of Peroxide Valuesupporting

confidence: 75%

“…The stability of cattle. Pradhan, Rhee, & Hernandez (2000) found catalase in refrigerated turkey varied with the type of higher catalase activity in pork LD muscle than in beef muscle (Renerre et al, 1999). Our study has LD muscle.…”

Section: Determination Of Peroxide Valuementioning

confidence: 61%

See 2 more Smart Citations

Correlation between acid, TBA, peroxide and iodine values, catalase and glutathione peroxidase activities of chicken, cattle and camel meat during refrigerated storage

Gheisari¹

2011

Vet. World

View full text Add to dashboard Cite

The aim of this study was correlation determination between fat putrefaction indices and antioxidative enzymes in chicken, cattle and camel meat during refrigerated storage. Longissimus dorsi muscle of three Iranian dromedary one humped camel and three Holstein cattle and breast muscle of three broiler breeder chicken were obtained from the carcasses 3 days postmortem. The samples were ground and stored at 4 °C for 0, 2, or 4 days. Peroxide, TBA, acid and iodine values, catalase and glutathione peroxidase (GSH-Px) activities of the muscles were performed in each storage time. Catalase and GSH-Px activities were much higher in camel than in chicken and cattle and higher in cattle than in chicken. TBA value was lower in chicken than in camel. Camel had higher acid value than cattle. Chicken showed the highest and camel had the lowest iodine values. Catalase and GSH-Px activities and iodine values were quite stable during refrigerated storage. Acid values increased significantly over storage days in cattle. During the 4-day storage period, TBA and peroxide values increased. GSH-Px activity showed negative correlation with acid and TBA values in chicken and cattle. Acid value (for chicken and cattle) and peroxide value (for 3 animal species) showed positive correlation with TBA content. Iodine value had positive correlation with catalase activity in cattle and negative correlation with peroxide and TBA values in camel. In conclusion, our results indicate that peroxide and TBA values can be used as lipid quality indices in chicken, cattle and camel meat during 4 day storage in refrigerator.

show abstract

Section: Determination Of Peroxide Valuecontrasting

confidence: 96%

Section: Determination Of Peroxide Valuesupporting

confidence: 75%

See 1 more Smart Citation

Correlation between acid, TBA, peroxide and iodine values, catalase and glutathione peroxidase activities of chicken, cattle and camel meat during refrigerated storage

Gheisari¹

2011

Vet. World

View full text Add to dashboard Cite

show abstract

“…Sarcoplasmic proteins play a critical role in fresh meat color due to their ability to interact directly with myoglobin (Renerre et al, 1996), and the role of sarcoplasmic proteome on muscle-specific beef color stability has been reported previously. Joseph et al (2012) compared the sarcoplasmic proteome of color-stable longissimus lumborum (LL) and color-labile psoas major (PM), and reported differential abundance of several proteins, including metabolic enzymes, antioxidant proteins, and chaperones.…”

mentioning

confidence: 80%

“…In general, oxidative muscles (such as PM) have greater activities of superoxide dismutase and catalase than glycolytic muscles (Terevinto et al, 2010). Renerre et al (1996) reported that the increase in the activities of the antioxidant enzymes of color-labile muscles such as PM and diaphragm could be a defensive mechanism to the increased oxidative stress in such muscles during postmortem.…”

Section: Antioxidant Proteinsmentioning

confidence: 99%

Changes in the Sarcoplasmic Proteome of Beef Muscles with Differential Color Stability during Postmortem Aging

Nair

Beach

et al. 2018

Meat and Muscle Biology

View full text Add to dashboard Cite

Beef color is a muscle-specific trait, and sarcoplasmic proteome influences muscle-specific variations in beef color stability. Postmortem aging influences the color and sarcoplasmic proteome of beef muscles. Nonetheless, muscle-specific changes in sarcoplasmic proteome of beef muscles with differential color stability during aging have not been characterized yet. Therefore, our objective was to examine the changes in the sarcoplasmic proteome of 3 differentially color stable muscles from beef hindquarters during postmortem aging. Longissimus lumborum (LL), psoas major (PM), and semitendinosus (ST) separated from 8 (n = 8) beef carcasses (24 h postmortem) were subjected to aging in vacuum packaging (2°C) for 0, 7, 14, and 21 d. On each aging day, steaks were fabricated, and allotted to refrigerated storage (2°C) under aerobic packaging. Samples for proteome analysis obtained during fabrication were frozen at –80°C. Instrumental color and metmyoglobin reducing activity were evaluated on d 0, 3, and 6 of storage. Sarcoplasmic proteome was analyzed, and differentially abundant proteins were identified using mass spectrometry. Color attributes and biochemical parameters were influenced by muscle source and aging (P < 0.05); LL and ST had greater (P < 0.05) surface redness than PM. Aging also influenced surface redness, with 7-d aged steaks demonstrating greatest values (P < 0.05). Proteome analysis identified 135 protein spots differentially abundant (P < 0.05) between the muscles and aging time points indicating muscle-specific changes during aging. The identified proteins included glycolytic enzymes, proteins associated with energy metabolism, antioxidant proteins, chaperones, and transport proteins. Overall, the glycolytic enzymes were more abundant (P < 0.05) in color-stable muscles and at aging times with greater color stability, indicating that these proteins could be used as potential biomarkers for beef color.

show abstract

Shelf‐life extension of refrigerated seabass slices under modified atmosphere packaging

2002

View full text Add to dashboard Cite

The effect of CO 2 -enriched atmosphere in combination with either oxygen or nitrogen on the keeping quality of seabass slices stored at 4°C was investigated. The inhibitory effect on bacterial growth increased proportionally to the CO 2 concentration in the packaging, maximum inhibition being achieved with 100% CO 2 (P < 0.05). Seabass slices stored in CO 2 -enriched atmosphere had lower total volatile base, trimethylamine, ammonia and formaldehyde contents than those stored in air (P < 0.05). However, increases in lightness and exudate loss were observed for samples packaged in high-CO 2 atmosphere, suggesting the denaturation of both muscle and pigment proteins by carbonic acid formed. Thiobarbituric acid-reactive substances (TBARS) increased as the CO 2 concentration increased (P < 0.05). However, odour,¯avour and overall acceptability of CO 2 -enriched packaged samples, particularly with 80 and 100% CO 2 , were acceptable throughout storage for 21 days. Chemical and microbial changes in all samples were generally in agreement with sensory panel evaluations. The shelf-life of seabass slices packaged in 80±100% CO 2 atmosphere could be extended to more than 20 days at 4°C, compared with 9 days for those packaged in air.

show abstract

Antioxidant enzyme activities in beef in relation to oxidation of lipid and myoglobin

Cited by 165 publications

References 30 publications

Correlation between acid, TBA, peroxide and iodine values, catalase and glutathione peroxidase activities of chicken, cattle and camel meat during refrigerated storage

Correlation between acid, TBA, peroxide and iodine values, catalase and glutathione peroxidase activities of chicken, cattle and camel meat during refrigerated storage

Changes in the Sarcoplasmic Proteome of Beef Muscles with Differential Color Stability during Postmortem Aging

Shelf‐life extension of refrigerated seabass slices under modified atmosphere packaging

Contact Info

Product

Resources

About