Bioanalytical methods for the metalloproteomics study of bovine longissimus thoracis muscle tissue with different grades of meat tenderness in the Nellore breed (Bos indicus)

Baldassini, Welder Angelo; Braga, Camila Pereira; Chardulo, Luis Artur Loyola; Silva, Josineudson Augusto Ii Vasconcelos; Malheiros, Jessica Moraes; Albuquerque, Lúcia Galvão de; Fernandes, Talita Tanaka; Padilha, Pedro M.

doi:10.1016/j.foodchem.2014.07.131

Cited by 33 publications

(15 citation statements)

References 24 publications

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“…The increase in the MFI values over periods of aging could be attributed to enhance proteolysis by calpains and resulting increased tenderness. In this study, the increase in the myofibrillar fragmentation index values post mortem in this study is in agreement with observations of Baldassini et al (). The direct comparison of data with those from literature is difficult as myofibrillar fragmentation is greatly influenced by breed (Marino et al, ), aging time (Dosler, Polak, Zlender, & Gasperlin, ) and process of homogenization (Hopkins, Littlefield, & Thompson, ).…”

Section: Resultssupporting

confidence: 93%

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: 93%

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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“…To represent each RFI groups (high vs. low), a pooled of liver samples was created from equal amounts of tissue and, subsequently, this standard was used for protein extraction and electrophoresis procedures. Briefly, approximately 375 µg of protein extracts were loaded into first dimension strips (13 cm) and the protein extracts were separated on pH 3-10 gradient as previously described [11]. After this step, the focusing strips were placed on a polyacrylamide gel with a concentration of 12.5% (w/v) in the second dimension of the electrophoretic process was performed in the molecular weight (MW) range of 14-97 kDa.…”

Section: Two-dimensional Electrophoresismentioning

confidence: 99%

“…The gels from RFI groups were scanned and the images analyzed using the ImageMaster Platinum (v. 7.0) as previously described [11,12] with minor adaptations. In brief, the equivalent spots (matching) were identified, and automatic and manual editing was performed to remove false spots.…”

Section: Image Analysismentioning

confidence: 99%

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Proteomic investigation of liver from beef cattle (Bos indicus) divergently ranked on residual feed intake

et al. 2018

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Proteomics studies can be used to identify proteins that affect feed efficiency traits, related to cost and profitability of meat production. We used a proteomic approach based on two-dimensional electrophoresis (2D-PAGE) in combination with mass spectrometry (ESI-MS) to study liver samples of Nellore bulls divergently ranked according to residual feed intake (RFI). The study showed that 71 protein spots were expressed differentially (P < 0.05) among RFI groups and 47 were identified by ESI-MS. In RFI, efficient animals (low RFI) eat less than predictions, based on their weights and growth rate, while inefficient animals (high RFI) that eat more than predicted. Data from 18 animals (9 high vs. 9 low RFI) aged 24-26 months in feedlot finishing were used. Immediately after slaughter, liver samples were collected and protein extracts were separated. The gels of RFI groups were scanned and the images analyzed, whereby we found 279 and 215 liver protein spots in high and low RFI bulls, respectively. The proteins identified were related to the following biological functions: (I) oxygen transport and blood flow; (II) mitochondrial function and energy metabolism; (III) amino acid metabolism, ion transport, and cell survival. The study suggests hemoglobin subunit beta and heat shock protein 71 kDa and as molecular markers to study FE in Nellore cattle. Moreover, proteins such as 3-ketoacyl-CoA thiolase and glutamate dehydrogenase 1 were found in liver from high and low RFI animals, respectively. Such protein expression could be associated with changes in the oxidative capacity of RFI phenotypes.

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“…Advanced technique such as metalloproteomics (Baldassini et al, 2015) has been utilized to examine meat quality in Zebu cattle (Bos indicus, Nellore breed). Interestingly, this approach utilized traditional 2-DE followed by the characterization of calcium ions in protein spot utilizing X-ray fluorescence as well mass spectrometric (ESI-MS) determination of candidate proteins.…”

Section: Proteomic Approaches In Meat Quality Researchmentioning

confidence: 99%

Application of proteomics to characterize and improve color and oxidative stability of muscle foods

Joseph¹,

Nair

Suman

2015

Food Research International

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Bioanalytical methods for the metalloproteomics study of bovine longissimus thoracis muscle tissue with different grades of meat tenderness in the Nellore breed (Bos indicus)

Cited by 33 publications

References 24 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

Proteomic investigation of liver from beef cattle (Bos indicus) divergently ranked on residual feed intake

Application of proteomics to characterize and improve color and oxidative stability of muscle foods

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