Effect of Combined High Pressure and Thermal Treatment on Myofibrillar Proteins Solubilization of Beef Muscle
نویسندگان
چکیده
The effects of high pressure (to 600 MPa) at different temperatures (20 to 60 °C) for 20 min on protein solubilization and electrophoretic pattern in beef post-rigor longissimus dorsi muscle were studied. The results showed that protein solubilization increased with increasing temperature, especially from 40 °C to 60 °C. A regular trend of protein solubilization was found when isolated myofibrils were subjected to high pressure at different temperatures, an increase was observed with increasing pressure up to about 400 MPa, solubility then decreasing to 600 MPa. Electrophoretic profiles showed that myosin light chains and actin thin filaments were sensitive to pressure, and were released from myofibrils subjected to 100 MPa and higher pressures at the different temperatures.
منابع مشابه
Proteins and proteolytic activity changes during refrigerated storage in sea bass (Dicentrarchus labrax L.) muscle after high-pressure treatment
Contrary to other preservation methods like thermal treatments, high pressure can destroy microorganisms without affecting the nutritional quality, color, or food texture. The firm texture of fish flesh is an important quality parameter. During the refrigerated storage, the tissue becomes softer and the muscle is deteriorated by different proteases. The aim of this study was to study the modifi...
متن کاملThe shelf-life of conventional surimi and recovery of functional proteins from silver carp (Hypophthalmichthys molitrix) muscle by an acid or alkaline solubilization process during frozen storage
The shelf-life of conventional surimi and isolated proteins that modified by acidic pH (2.5) and by using alkali pH (11) from silver carp (Hypophthalmichthys molitrix) was studied during months of storage at -18±2 °C. For conventional surimi, three washing steps were used. In the third stage of washing, 0.2% NaCl was used to withdraw more water. The result showed that isolated protein by alkali...
متن کاملThe Extractability of Inner-Membrane Proteins from Salmonella typhimurium Intact Cells, Spheroplasts and Inner-Membrane Fragments by Non-Denaturing Detergents
The effect of Triton X-100, Na cholate and Tween 80 on the solubilization of integral membrane proteins in intact cells, spheroplasts and inner-membrane fragments of Salmonella typhimurium was studied. The detergents were used in various concentrations (1.6 to 64 mM) and cytochromes b and d were used as marker to monitor the solubilization of membrane-bound proteins. Results showed that no inne...
متن کاملShort communication:Effect of salt and alkaline on the physicochemical properties of the protein isolates extracted from lanternfish (Benthosema pterotum)
Food proteins have long been recognized for their nutritional and functional properties. The nutritional properties of proteins are associated with their amino acid content. On the other hand, the functional properties of proteins relate to their contribution to the physiochemical and sensory properties of foods (Sila and Bougatef, 2016). Marine organisms contain proteins with high quantities o...
متن کاملChemical changes and shelf-life of conventional surimi and proteins recovered using pH change method from common carp (Cyprinus carpio) muscle during 5 months storage at -18ºC
Chemical changes and shelf-life of common carp (Cyprinus carpio) surimi prepared by conventional washing method and solubilization by acid and alkali processes were investigated during 5 months of storage at -18 °C. Results showed that surimi produced with acid and alkaline solubilization is significantly higher yield than the conventional surimi. Protein solubilization by using acid and alkali...
متن کامل