2D DIGE/MS to investigate the impact of slaughtering techniques on postmortem integrity of fish filet proteins

Addis, Maria Filippa; Pisanu, Salvatore; Preziosa, Elena; Bernardini, Giovanni; Pagnozzi, Daniela; Roggio, Tonina; Uzzau, Sergio; Saroglia, Marco; Terova, Genciana

doi:10.1016/j.jprot.2012.04.021

Cited by 31 publications

(15 citation statements)

References 29 publications

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“…In recent years, the increasing number of proteomic studies have provided insight into the biochemical processes occurring post-mortem in fish species (Addis, Cappuccinelli, Tedde, & Pagnozzi, 2010;Addis et al, 2012;Alves, Cordeiro, Silva, & Richard, 2010;Delbarre-Ladrat, Cheret, Taylor, & Verrez-Bagnis, 2006;Forne, Abia, & Cerda, 2010), thus facilitating the identification of the markers of fish muscle quality. The 2-D PAGE/MS identification approach is very well suited for studies on degradation patterns and also enables information to be obtained on the molecular weight and isoelectric point of the protein spots of interest.…”

Section: Introductionmentioning

confidence: 99%

Effects of tea polyphenols on the post-mortem integrity of large yellow croaker (Pseudosciaena crocea) fillet proteins

Zhao

Wang

et al. 2013

Food Chemistry

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Section: Introductionmentioning

confidence: 99%

Effects of tea polyphenols on the post-mortem integrity of large yellow croaker (Pseudosciaena crocea) fillet proteins

Zhao

Wang

et al. 2013

Food Chemistry

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“…According to our study DSC results, the transition peak I was myosin, II sarcoplasmic proteins‐ with collagen, and peak III as actin (Addis et al, ; Akköse, ; Hastings, Rodger, Park, Mathews, & Anderson, ; Howell, Matthews, & Donelly, ). The peak I, myosin degradation in the degradation of the observed proteins in fish meat, is associated with collagen and sarcoplasmic breakdown between the second pass and the final peak with actin cast (Vasquez Mejia et al, ).…”

Section: Resultsmentioning

confidence: 54%

Determining protein denaturation of sardine (Sardina pilchardus) marinates before and after the maturation

Dericioglu

Alak

Atamanalp

2019

J Food Process Preserv

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In this study, sardine fish (Sardina pilchardus) was subjected to marination at different degrees of acidity (2.5%–5%). On the basis of the duration of maturation (22 days) and postmaturation period (three months after maturation), protein denaturation and quality changes of marinades were determined. Quality parameters, such as pH, acidity, salinity, and lipid oxidation, were examined for both periods. As a result of the study carried out for 22 days at different acidity levels, the change in the amount of TVB‐N was found to be insignificant (p > 0.05), but the differences in pH, TBARS, acidity, and salinity levels were found to be significant (p < 0.05). In the postmaturation period, the change in the TBARS amount was insignificant (p > 0.05), and the other parameters were found to be significant (p < 0.05). SDS‐PAGE analysis showed that fish muscle and brine proteins showed different profiles and a decrease in densities of MHC, actin, and TM bands during the maturation period was observed. Practical applications Protein denaturation is important in fisheries products, so multiple verification tests should be performed to monitor this process. It was suggested that DSC and SDS‐PAGE techniques are easier and quicker analyses for determining protein denaturation in seafood products compared with traditional techniques.

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“…The silver staining revealed 100 to 200 differential protein spots which were marked with different alphabet in the patterns, 139 (2 days), 138 (4 days), 192 (6 days), and 151 (8 days), respectively, when expression of 1.5‐fold or more difference in spot gray value. The results indicated that changes occurred in the overall protein composition during the refrigerated storage, and the variation in protein abundance appeared to be significantly correlation with storage time (Addis et al., ). Due to the role of endogenous protease and microorganism in muscles, the muscle protein was degraded, meanwhile the differential protein spots on the map showed varying degrees of change.…”

Section: Resultsmentioning

confidence: 98%

The Discovery of Proteins Associated with Freshness of Coregonus Peled Muscle During Refrigerated Storage

Deng

Lei

et al. 2019

Journal of Food Science

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The aim of this study is to identify the protein indicator of freshness of Coregonus peled using two‐dimensional gel electrophoresis (2‐DE) and matrix‐assisted laser desorption ionization‐time‐of‐flight/time‐of‐flight mass spectrometry (MALDI‐TOF/TOF MS) methods. Samples were obtained prior to (control group) and 2, 4, 6, and 8 days after refrigerated storage for quality and proteomics analysis. Three proteins were found to have significant differential abundance in sample groups during the refrigerated storage, including l‐lactate dehydrogenase, adenylate kinase isoenzyme 1, and myosin heavy chain, which were associated with freshness changes of C. peled. The freshness of C. peled fish during the refrigerated storage can be differentiated from the comparison of the specific proteins. Practical Application The changes of food quality pose not only the relative economical loses but also the potential implications on consumer's health. Proteomics can represent a powerful tool to explore potential biomarkers that may be related to meat quality defects. The identification of key protein biomarkers linked to freshness of Coregonus peled allows to monitor the response of the food matrix during storage and try to minimizes these defects.

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2D DIGE/MS to investigate the impact of slaughtering techniques on postmortem integrity of fish filet proteins

Cited by 31 publications

References 29 publications

Effects of tea polyphenols on the post-mortem integrity of large yellow croaker (Pseudosciaena crocea) fillet proteins

Effects of tea polyphenols on the post-mortem integrity of large yellow croaker (Pseudosciaena crocea) fillet proteins

Determining protein denaturation of sardine (Sardina pilchardus) marinates before and after the maturation

The Discovery of Proteins Associated with Freshness of Coregonus Peled Muscle During Refrigerated Storage

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