MYOFIBRILLAR AND SARCOPLASMIC PROTEIN OXIDATION AND DEGRADATION OF THIN‐LIPPED GRAY MULLET (<i>LIZA RAMADA</i>) DURING REFRIGERATED STORAGE (4C)

Tokur, Bahar; Polat, Abdurrahman

doi:10.1111/j.1745-4573.2009.00170.x

Cited by 11 publications

(10 citation statements)

References 48 publications

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“…One of the main consequences of protein oxidation is to form protein aggregates or protein fragments under certain circumstances (Park et al ., ). During refrigerated storage, high‐molecular weight polymers via disulphide cross‐linking and/or degradation/digestion by proteolysis might be formed in the myofibrillar proteins (Tokur & Polat, ). Ali et al .…”

Section: Resultsmentioning

confidence: 99%

“…One of the main consequences of protein oxidation is to form protein aggregates or protein fragments under certain circumstances (Park et al, 2006). During refrigerated storage, high-molecular weight polymers via disulphide cross-linking and/or degradation/digestion by proteolysis might be formed in the myofibrillar proteins (Tokur & Polat, 2010). Ali et al (2015) studied the effects of repeated freeze-thaw cycles (0-6) on the SDS-PAGE banding patterns of myofibrillar proteins of chicken breast and observed slight degenerations in myosin and actin.…”

Section: Sds-page Analysis Of Myofibrillar Proteinmentioning

confidence: 99%

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Effects of different thawing methods on the quality of chicken breast

Zhang

Gao

Song

et al. 2017

Int J of Food Sci Tech

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Summary Freezing and thawing technologies are widely used in meat industry. This study aimed to investigate the effects of freezing and different thawing methods (Control group, CG; water immersing thawing, WT; low temperature combined with high‐humidity thawing, LT; combined thawing 1 (WT 15 min, then LT), CT1; combined thawing 2 (LT 2 h, then WT), CT2) on the quality of chicken breast. The results showed that all thawing methods significantly increased shear force value, the gap between muscle fibres, the contents of malondialdehyde (MDA) and carbonyl compounds, meanwhile, decreased the pH, CIE a* value, total protein solubility and sarcoplasmic protein solubility, compared with CG (P < 0.05). Among different thawing methods, LT was most effective in decreasing thawing loss but it had the highest contents of MDA and carbonyl compounds (P < 0.05). CT1 significantly decreased shear force value and MDA content (P < 0.05). Overall, freezing and thawing process had a detrimental effect on the quality of chicken breast, and the extent was pronounced with different thawing methods. On the basis of shortening thawing time and keeping meat quality, the results of this study suggested that CT1 could be chosen as the better thawing method.

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Section: Resultsmentioning

confidence: 99%

Section: Sds-page Analysis Of Myofibrillar Proteinmentioning

confidence: 99%

Effects of different thawing methods on the quality of chicken breast

Zhang

Gao

Song

et al. 2017

Int J of Food Sci Tech

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“…The formation of carbonyl compounds from amino acid side chains is well documented and probably the most outstanding result of metal ion‐catalyzed oxidation of MP 29. The quantification of carbonyl compounds by using the routine DNPH method has been widely employed as a general measure of Pox in multiple muscle foods (reviewed by Estévez and colleagues, 4) including fish muscle and fish products 33, 34, fresh meat 12, 14, 35 and a variety of meat products 19, 36, 37. Recently, Estévez and colleagues 8 identified specific carbonyl compounds in oxidized MP namely, α‐aminoadipic and γ‐glutamic semialdehydes (AAS and GGS, respectively) in oxidized MP by using HPLC‐MS.…”

Section: Muscle Protein Oxidation Mechanismsmentioning

confidence: 99%

Protein oxidation in muscle foods: A review

Lund

Heinonen

Baron

et al. 2010

Molecular Nutrition Food Res

823

636

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Protein oxidation in living tissues is known to play an essential role in the pathogenesis of relevant degenerative diseases, whereas the occurrence and impact of protein oxidation (Pox) in food systems have been ignored for decades. Currently, the increasing interest among food scientists in this topic has led to highlight the influence that Pox may have on meat quality and human nutrition. Recent studies have contributed to solid scientific knowledge regarding basic oxidation mechanisms, and in advanced methodologies to accurately assess Pox in food systems. Some of these studies have provided insight into the reactions involved in the oxidative modifications undergone by muscle proteins. Moreover, a variety of products derived from oxidized muscle proteins, including cross-links and carbonyls, have been identified. The impact of oxidation on protein functionality and on specific meat quality traits has also been addressed. Some other recent studies have shed light on the complex interaction mechanisms between myofibrillar proteins and certain redox-active compounds such as tocopherols and phenolic compounds. This paper is devoted to review the most relevant findings on the occurrence and consequences of Pox in muscle foods. The efficiency of different anti-oxidant strategies against the oxidation of muscle proteins is also reported.

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“…The other bands did not change and new bands also did not appear during 24 days of iced storage. The decrease of the bands intensity both in the presence and absence of reducing agent during post mortem storage could reflect to degradation and/or digestion of myofibriller and sarcoplasmic proteins by proteolysis during storage (Tokur and Polat, 2010;Ladrat et al, 2003;Lund and Lielsen, 2001;Benjakul et al, 1997). Enzymatic proteolysis of fish meat during post mortem storage cause disruption of the structure of the myofibrillar proteins (Jasra et al, 2001;Verrez-Bagnis et al, 1999) and is thought to cause post-mortem softening, which is one of the most important quality attributes of fish muscle during cold storage.…”

Section: Protein Denaturationmentioning

confidence: 99%

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Özoğul¹,

Küley²,

Tokur³

et al. 2011

Turk. J. Fish. Aquat. Sci.

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The quality of wild common sole (Solea solea) stored in ice was investigated by chemical (K value, biogenic amines, protein degradation (SDS and SDS-PAGE), pH, peroxide value (PV), free fatty acids (FFA), total volatile basic nitrogen (TVB-N), tiobarbituric acid (TBA) analyses), sensory (raw and cooked fish) and microbiological methods. The quality of common sole decreased on day 16 (fair quality-B) and they were no longer acceptable on day 20 (unacceptable quality-C). When common sole were considered as fair quality (B) by assessors on ~16-18 days, the average K value was ≥ 80%. Among the investigated biogenic amines, histamine was not detected. No major change in the protein profiles of common sole was observed. Sensory, microbial and biochemical results revealed that the shelf life of common sole was approximately ~16-18 days. Among the chemical parameters, the most consistent indicator to measure the change in freshness was K value that showed linear response with storage time.

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MYOFIBRILLAR AND SARCOPLASMIC PROTEIN OXIDATION AND DEGRADATION OF THIN‐LIPPED GRAY MULLET (LIZA RAMADA) DURING REFRIGERATED STORAGE (4C)

Cited by 11 publications

References 48 publications

Effects of different thawing methods on the quality of chicken breast

Effects of different thawing methods on the quality of chicken breast

Protein oxidation in muscle foods: A review

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