Effects of frozen-then-chilled storage on proteolytic enzyme activity and water-holding capacity of pork loin

Zhang, Yuemei; Ertbjerg, Per

doi:10.1016/j.meatsci.2018.07.017

Cited by 55 publications

(32 citation statements)

References 41 publications

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“…Casein zymography was performed according to Zhang & Ertbjerg (2018) with some modifications. Fish muscle (5 g) was homogenized (13500 rpm, 1 min) with 15 mL cold sample buffer (50 mM Tris, 5 mM ethylene diamine tetra acetic acid (EDTA), 10 mM α-thioglycerol, pH 7.4) and then centrifuged (10000 g × 20 min, 4 ℃) to get the supernatant.…”

Section: Casein Zymographymentioning

confidence: 99%

Protein degradation of black carp (Mylopharyngodon piceus) muscle during cold storage

et al. 2020

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The objective of this study was to investigate the effects of storage at different cold temperatures (4,-0.5,-3 and-20 ℃) on protein degradation and its relationship to structural changes of black carp muscle. At-0.5 and 4 ℃, microscopic studies showed that major structural changes included formation of gaps between myofibers and myofibrils, breakage of myofibrils and myofibers, and degradation of sarcoplasmic reticulum. Gel-based proteomic analysis showed that structural changes were accompanied by a degradation of a series of myofibrillar proteins, including titin, nebulin, troponin, myosin, myomesin, myosin binding protein, and α-actinin. And a loss of extractable gelatinolytic-and caseinolytic protease activities were also observed. At-3 and-20 ℃, formation of ice crystals was the most noticeable change. The study revealed the major proteins degraded at different locations in the black carp muscle, and the gelatinolytic-and caseinolytic proteases were suggested to contribute to those protein degradation.

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Section: Casein Zymographymentioning

confidence: 99%

Protein degradation of black carp (Mylopharyngodon piceus) muscle during cold storage

et al. 2020

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“…The function of one independent variable depends on the level of the others. If the interaction with each other is not conspicuous, it indicates that the main influence among each factor is independent of the other (Zhang & Ertbjerg, 2018; Biffin et al ., 2019). The different treatments (the number of F‐T cycle) were considered as fixed factors, and the three repeats were used as random factors.…”

Section: Resultsmentioning

confidence: 99%

Effect of multiple freeze‐thaw cycles on protein and lipid oxidation in rabbit meat

Wang

Zhang

et al. 2021

Int J of Food Sci Tech

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Summary Frozen storage is chosen to be the preferred method in meat preservation. However, multiple freeze‐thaw (F‐T) cycles will occur during the transfers or distribution processes under poor cold‐chain conditions. This study investigated the effects of multiple freeze‐thaw (F‐T) cycles on water mobility, microstructure damage, protein oxidation and lipid oxidation in rabbit meat during seven F‐T cycles through 56 days. Scanning electron microscopy results indicated that the increase of F‐T cycles induced the rupture of endomysia and the increase of gaps between fibres. Low‐field nuclear magnetic resonance (LF‐NMR) results showed that the peak area of T21 and T22 decreased with increasing number of repeated F‐T cycles, indicating that immobile water shifted to free water, and free water mobility increased. During repeated freeze‐thaw process, the peroxide value, thiobarbituric acid‐reactive substances, non‐haem iron content and carbonyl groups of rabbit meat gradually increased, whereas haem content, haem iron content and sulfhydryl content of rabbit meat gradually decreased. In addition, the results of Fourier transform infrared, sodium dodecyl sulphate polyacrylamide gel electrophoresis, and intrinsic fluorescence spectroscopy indirectly proved that multiple F‐T cycles could cause α‐helix structure disruption, protein aggregation and degradation, and tryptophan oxidation of rabbit meat myofibrillar protein (MP). Overall, multiple repeated F‐T cycles changed moisture migration, damaged microstructure and promoted lipid and protein oxidation of rabbit meat.

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“…As shown in Figure , the carbonyls content of MFPs increased with increasing of storage time, which total sulfhydryl decreased. The formation of carbonyls is one of the most significant changes in oxidated proteins, and sulfhydryl group is the most reactive functional group in MFPs and is easily oxidized into disulfide bond during storage (Chamba, Hua, & Katiyo, ; Zhang & Ertbjerg, ). The results showed that fish protein was gradually oxidized during the storage process, and thus affected meat freshness and quality.…”

Section: Resultsmentioning

confidence: 99%

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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Effects of frozen-then-chilled storage on proteolytic enzyme activity and water-holding capacity of pork loin

Cited by 55 publications

References 41 publications

Protein degradation of black carp (Mylopharyngodon piceus) muscle during cold storage

Protein degradation of black carp (Mylopharyngodon piceus) muscle during cold storage

Effect of multiple freeze‐thaw cycles on protein and lipid oxidation in rabbit meat

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

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