South African Journal of Animal Science
versión On-line ISSN 2221-4062
versión impresa ISSN 0375-1589
MOLOTO, K.W.; FRYLINCK, L.; STRYDOM, P.E. y KOORSEN, G.. Proteomics approach as a new way to predict tenderness as compared to the classical South African Beef Carcass Classification System. S. Afr. j. anim. sci. [online]. 2015, vol.45, n.3, pp.249-254. ISSN 2221-4062. http://dx.doi.org/10.4314/SAJAS.V45I3.3.
The current South African Beef Carcass Classification System classifies carcasses using physical attributes such as age, fatness code and the conformation of the carcass as the only indicator of tenderness, implying that optimal tender meat is obtained from carcasses from animals with no permanent teeth. Research shows that if we take modern technologies (use of beta-agonists, growth hormones and electrical stimulation amongst others) into account, this is not necessarily true. In this study m. longissimus lumborum samples were collected from Nguni breed animals, snap frozen and stored at -80 °C for further use in search of protein markers that can be used to predict tenderness in a non-invasive manner. Proteins were extracted in 1 mL TES buffer, isoelectrically focused on strips (pH 5 - 7) and separated by 2D SDS PAGE, stained with coomassie brilliant blue G250) and imaged by a Chemi-doc Mp imager. The results showed differences in protein expression, e.g. some proteins are present at 1 hour post mortem (Day 0) but absent at 3 days post mortem (Day 3). Other proteins showed an increase in expression as ageing progresses. These proteins correlated with myofibril fragments and Warner Bratzler changes which were measured. There are several factors that may be responsible for these changes in differential expression during ageing such as proteolytic action (i.e. calpains and calpastatin system, cathepsins) or maybe apoptosis. The proteins in the profiles of Nguni breed animals which showed differential expression in response to ageing are still to be determined.
Palabras clave : Nguni breed; protein markers for tenderness; two dimensional gel electrophoresis (2D SDS PAGE).