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American Journal of Biochemistry and Molecular Biology
Year: 2013  |  Volume: 3  |  Issue: 2  |  Page No.: 240 - 247

Ultrasonication of Chicken Natural Actomyosin: Effect on ATPase Activity, Turbidity and SDS-PAGE Profiles at Different Protein Concentrations

Riaz Ahmad and Absar-ul Hasnain    

Abstract: With the increasing application of ultrasonics in meat tenderization and processing, physicochemical events initiated by sonic radiation at myofibrillar level and propagated in complex tissue such as meat require a clear understanding. The enormous amount of basic information collected by studying myofibrils, actomyosin or their individual constituents has already clarified intricacies of muscular contraction and, part of such basic information has find application in meat sciences. In this investigation, chicken Natural actomyosin (NAM) has been taken as a simple model to work out some effects of ultrasonication in a concentration range of 0.5 to 1.8 mg protein mL-1. At each concentration, NAM solution in 0.6 M NaCl (2.0 mL) was individually exposed to 20 kHz sonic waves for a total of 10 min. Cooling was maintained by keeping NAM containers in crushed ice and a lag of 5 sec after each 10 sec long sonic burst. Aliquots from each sonicated NAM were subjected to biochemical analyses. Most striking differences were observed in Ca2+-ATPase activity, which displayed a steady decline that corresponded with the decreasing protein concentration. Ultrasonication of NAM for 10 min caused a loss of ~47% of Ca2+-ATPase activity at the highest dilution (0.5 mg mL-1). In the same order of protein concentration, turbidity of ultrasonicated NAM also decreased which denotes increasing transparency. Thus, ATPase and turbidity data demonstrate that due to sonic radiation, interactions among constituents of chicken actomyosin complex alter and these structural changes are devoid of any fragmentation. Under present experimental conditions, SDS-PAGE profiles did not reveal any novel band which could be attributed to ultrasonic fragmentation or proteolytic contamination. The findings also suggest that unlike myofibrils, actomyosin is a model where interactions and substructural changes of constituent polypeptides can be investigated without interference of endogenous muscle proteases.

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