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ATPase activities and autolysis of kuruma prawn Penaeus japonicus muscle proteins


 Soottawat Benjakul1*, Wonnop Visessanguan2, Tanong Aewsiri3, Munehiko Tanaka4,

Mehdi Nikoo5


1Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, 90112, Thailand

2National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Phaholyothin Road, Klong 1, Klong Luang, Pathumthani,12120, Thailand

3Food Science Division, Institute of Agricultural Technology, Walailak University, Nakornsrithammarat, 80160, Thailand

4Department of Food Science and Technology, Tokyo University of Marine Science and Technology, Konan 4, Minato, Tokyo 108-8477, Japan

5Food Laboratory, Mazandaan University of Medical Sciences, Sari, Iran


Received: 22 January 2011; Accepted: 2 March 2011




Ca2+-, Mg2+-, Mg2+,Ca2+- and Mg2+-EGTA-ATPase activities of natural actomyosin (NAM) from kuruma prawn (Penaeus japonicus) at different temperatures were determined. The maximal activities of all ATPase were observed at 35 °C and subsequently decreased with increasing temperatures. The loss in Ca2+-sensitivity was noticeable as the temperatures increased, suggesting the denaturation of regulatory proteins. The autolysis of kuruma prawn muscle was also investigated at different temperatures. The maximal autolytic activity was found at 60 °C. NaCl at higher concentrations exhibited the greater inhibitory effect toward autolysis. Metalloproteinase inhibitors including 1,10-phenanthroline, EDTA, EGTA and pyrophosphate at the range of 1-10 mM could inhibit the autolysis of kuruma prawn muscle as evidenced by the lower trichloroacetic acid-soluble peptide content and more myosin heavy chain (MHC) band intensity retained. The result suggested that heat-activated metalloproteinases involved in the autolysis of kuruma prawn muscle at the elevated temperatures. 


Keywords: ATPase, Natural actomyosin, Prawn, Muscle, Autolysis, Proteinase

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© 2011, IAU, Tonekabon, IAR-11-1106.


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