The effect of the packaging system and storage time on myofibrillar protein degradation and oxidation process in relation to beef tenderness

Moczkowska, Małgorzata; Półtorak, Andrzej; Montowska, Magdalena; Pośpiech, E.; Wierzbicka, Agnieszka

doi:10.1016/j.meatsci.2017.03.008

Cited by 57 publications

(53 citation statements)

References 46 publications

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“…Muscle did not show explicit differences in the ash content. The results of the basic composition for individual muscles are in accordance with the results obtained by Marino et al () and Moczkowska et al (). PM as an oxidative muscle, not very active during the life of animal, is characterized by a higher fat content and a lower moisture content than longissimus muscles, which is confirmed by the results obtained by Canto et al ().…”

Section: Resultssupporting

confidence: 92%

“…After nonlinked antibodies were washed out, membrane was incubated with the secondary antibody marked with alkaline phosphatase for 1 hr in room temperature (Anti‐Mouse IgG Alkaline Phosphatase antibody produced in the goat affinity isolated antibody, dilution 1:30,000, Sigma Aldrich, Sigma Aldrich, Inc.). After secondary antibodies were washed out (3× TBST) streaks were detected by inducing colorimetric assay with NBT/BCIP (Moczkowska, Półtorak, Montowska, Pospiech, & Wierzbicka, ).…”

Section: Methodsmentioning

confidence: 99%

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The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

Onopiuk

Półtorak

Wierzbicka

2018

J Food Process Preserv

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The impact of muscle and aging time on meat tenderness in carcasses of Limousin × Holstein‐Friesian bulls was evaluated. The scope of the research covered measurement of pH, basic composition, total collagen, shear force (WBSF), myofibrillar fragmentation index (MFI), and analysis of proteins with the use of SDS‐PAGE electrophoresis. The results underline the strong relationship between the chemical composition and collagen content of meat and its tenderness. The MFI as an index of advancement of the myofibrillar degradation process showed a high correlation with the instrumentally estimated shear force. In all muscles, a decrease of desmin, troponin T (TnT) and an increase of TnT derived polypeptides during aging were observed. The highest decrease of TnT together with the decrease WBSF in Semitendinosus (ST) muscles during aging resulted from a more extensive proteolysis in this muscle. The results indicate the relationship between the activity of selected proteins and the shear force, which may lead to a more effective prediction of meat tenderness. Practical applications Beef aging is an important process of preparing beef for consumption. Based on the results presented in this paper one may state that the phenomenon of bovine meat (Limousin × Holstein‐Friesian crossbred bulls) tenderness during post mortem aging is considerably related to the quality and quantity scope of changes on myofibrall proteins, mainly desmin, troponin T and proteins with molecular weight of 32‐27 kDa. The obtained results proved that meat tenderness and proteolytic changes during aging are related to the type of muscle, its function and location in the carcass. The results show a strong relationship between the activity of selected proteins and shear force value, which confirms by high correlation coefficients. Analysis of muscle proteins during aging is necessary to understand the biological basis of changes in meat tenderness and their differences among muscles. The information available in the current study should be very useful to the meat industry for prediction of beef quality especially beef tenderness during the aging process.

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Section: Resultssupporting

confidence: 92%

Section: Methodsmentioning

confidence: 99%

The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

Onopiuk

Półtorak

Wierzbicka

2018

J Food Process Preserv

Self Cite

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“…By using 2D diagonal-PAGE, Kim et al (2010) obtained results suggesting that intermolecular cross-linking might have occurred between myosin heavy chain and titin. Cross-linked myosin heavy chain has been observed as a major oxidation product in high oxygen packaged meat in other studies as well (Bao and Ertbjerg 2015;Bao et al 2016;Moczkowska et al 2017;Rysman et al 2014).…”

Section: Cross-linking Of Structural Proteinsmentioning

confidence: 63%

Effects of protein oxidation on the texture and water-holding of meat: a review

Bao

Ertbjerg

2018

Critical Reviews in Food Science and Nutrition

138

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Protein oxidation readily occurs in postmortem muscle during storage and processing. Over the past decade new analytical methods have been developed and new aspects of protein oxidation in meat have been studied, such as the reaction mechanism, and impacts on eating quality and nutritional value. It is now evident that amino acid side chains in myofibrillar proteins undergoes modifications due to oxidative stress. In turn this will lead to formation of new protein-protein cross-links in structural proteins, however, also the overall level of fixed-charge groups attached to the peptide backbones is modified. Meat texture and water-holding are important quality attributes and they are affected by the oxidation of structural proteins. Different mechanisms have been suggested to explain the oxidation-induced quality changes, focusing mainly on reduced proteolysis and formation of cross-links. This review explores the current understanding of protein oxidation in fresh meat in relation to texture and water-holding. The consequences of protein oxidation at molecular level in relation to oxidation-induced cross-linking and changes in net charges of myofibrillar proteins, and the impacts on texture and water-holding are discussed.

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“…Furthermore, the meat structure became progressively loose during aging which was probably due to the weakening of myofibrillar structures. [25,26] More FAAs may release from meat to broth during heating. This led to an increase in the concentration of FAAs in broth.…”

Section: Free Amino Acidsmentioning

confidence: 99%

Effect of postmortem aging time on flavor profile of stewed pork rib broth

Hou

Liu

2018

International Journal of Food Properties

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The objective of this study was to investigate changes in flavor components in broth prepared by pork ribs that were aged for 1 d, 3 d, and 7 d. The contents of free amino acids (FAAs), nucleic acid-related compounds, organic acids, and volatile compounds in broth were measured. The overall taste and aroma profiles were evaluated by electronic tongue, electronic nose, and sensory panelists. The results showed that the FAAs and succinic acid contents increased, while the 5ʹ-guanosine monophosphate, 5ʹ-inosine monophosphate, and 5ʹ-adenosine monophosphate contents decreased as the aging time increased. These changes led to the taste characteristics of broth being more savory. However, the results of gas chromatography-mass spectrometry, electronic nose, and sensory test all showed that there were no significant differences in aroma among the samples, where the main volatile compounds of broth were aldehydes, including hexanal, nonanal, octanal, heptanal, (Z)-2-heptanal, and (E)-2-decenal. Hence, postmortem aging affected the taste rather than the aroma of pork rib broth, and extending aging time can improve the taste of broth.

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The effect of the packaging system and storage time on myofibrillar protein degradation and oxidation process in relation to beef tenderness

Cited by 57 publications

References 46 publications

The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

Effects of protein oxidation on the texture and water-holding of meat: a review

Effect of postmortem aging time on flavor profile of stewed pork rib broth

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