RESUMEN
The mechanisms by which electrical stimulation (ES) of carcasses can be used to modulate meat quality are reviewed. Evidence to support an effect of ES on tenderness (and other meat quality attributes) based solely on changes in the pH/temperature profile within carcass muscles are presented. The interactions between electrical parameters and the contraction responses of carcass muscles are described to provide generalised principles to guide the design of electrical stimulation technology. The commercial risks to meat quality of inappropriate use of electrical stimulation, particularly excessive stimulation to produce PSE-like conditions, are considered.
RESUMEN
Ensuring meat quality attributes meet the requirements of the diverse range of markets is a critical component for the continued success of the New Zealand and Australian meat industries. Developing cost-effective and flexible technologies to help meet this requirement is a central objective of a current Meat and Wool New Zealand and Meat and Livestock Australia funded programme. This initiative was developed three years ago; it is a collaborative programme that involves meat scientists, electrical engineers and commercial meat processors. To ensure this programme successfully delivers technologies and knowledge to the Australasian meat industry, the following strategies have been developed: measurement of meat quality attributes 'on-line' during processing; development of 'expert systems' that can integrate and interpret on-line measurements and development of quality-related feedback systems from the market that can be fed back to producers; and, development of methods to manipulate structural and biochemical events in meat to create new commercial opportunities for both producers and processors. This paper gives an overview of some of the new technologies that have developed from this programme that are being used commercially or, are undergoing the final stages of commercial validation.
RESUMEN
This paper describes the colour properties of seven hot-boned, unstimulated beef striploins during rigor attainment at 9, 14 and 24°C, during blooming at 4°C, and after storage at -1°C for 0, 2 and 8 weeks. Immediately after rigor attainment (0 weeks of storage) full blooming, as judged by L* and chroma, took at least 12 h. After 2 and 8 weeks storage, blooming was complete within about 4 h. The exponential equations describing blooming were different for 0 weeks compared with 2 and 8 weeks. This difference can be explained in terms of oxygen consumption by meat freshly in rigor. At 0 weeks, meat that entered rigor at 24°C had the best bloomed colour, whereas at 2 and 8 weeks the 9°C treatment had the best and the 24°C the worst. The data set, which spanned a range of ultimate pH values and three rigor attainment temperatures, was used to estimate the value of early colour measurements (first 24 h post-rigor) in predicting colour during display several weeks later. As judged by correlation coefficients, early measurements of hue were the only ones useful. L* and chroma were poor predictors. This result, together with the knowledge that blooming is slow in the first 24 h post-rigor, casts doubt on the value of subjective or objective colour assessments made in chillers. Temperature of rigor attainment between 9 and 24°C did not affect the time of browning onset, nor the rate of browning. It was confirmed that meat with lower pH had higher chroma before and after blooming.
RESUMEN
Maize actin-depolymerizing factor, ZmADF, binds both G- and F-actin and enhances in vitro actin dynamics. Evidence from studies on vertebrate ADF/cofilin supports the view that this class of protein responds to intracellular and extracellular signals and causes actin reorganization. As a test to determine whether such signal-responsive pathways existed in plants, this study addressed the ability of maize ADF to be phosphorylated and the likely effects of such phosphorylation on its capacity to modulate actin dynamics. It is shown that maize ADF3 (ZmADF3) can be phosphorylated by a calcium-stimulated protein kinase present in a 40-70% ammonium sulphate fraction of a plant cell extract. Phosphorylation is shown to be on Ser6, which is only one of nine amino acids that are fully conserved among the ADF/cofilin proteins across distantly related species. In addition, an analogue of phosphorylated ZmADF3 created by mutating Ser6 to Asp6 (zmadf3-4) does not bind G- or F-actin and has little effect on the enhancement of actin dynamics. These results are discussed in context of the previously observed actin reorganization in root hair cells.
Asunto(s)
Actinas/metabolismo , Calcio/fisiología , Proteínas de Microfilamentos/metabolismo , Proteínas Quinasas/metabolismo , Serina/metabolismo , Zea mays/metabolismo , Factores Despolimerizantes de la Actina , Secuencia de Aminoácidos , Destrina , Gelsolina/metabolismo , Cinética , Proteínas de Microfilamentos/genética , Datos de Secuencia Molecular , Mutagénesis Sitio-Dirigida , Fosforilación , Extractos Vegetales/metabolismo , Unión Proteica , Proteínas Recombinantes/metabolismoRESUMEN
The effect of dietary supplementation with clenbuterol for either 8 days or 55 days in lambs was studied. The 55-day treatment was combined with an immediate preslaughter exercise regime. The effect of these treatments on post-mortem calpain system activities, meat ageing and meat quality was studied. Neither short-nor long-term supplementation had an effect on the rate of pH fall post mortem. Short-term supplementation had no effect on the initial nor the final shear force values but these were higher at intermediate times. In contrast, prolonged supplementation increased shear force values at all times post mortem. Preslaughter exercise, while influencing the rate of pH decrease in both control and supplemented groups, did not affect meat tenderness. After short-term clenbuterol-supplementation, the in-vitro µ-calpain activity was significantly lower in the supplemented group at 6 and 24 hr post mortem, while m-calpain and calpastatin activities were largely unaffected. In contrast, 55-day clenbuterol supplementation resulted in significantly higher levels of calpastatin activity at all times post mortem. These data imply that clenbuterol results in toughened meat due to alterations in the calpain/calpastatin system, the mechanisms of which are dependent upon the duration of supplementation.