ATPase activities and autolysis of kuruma prawn Penaeus japonicus muscle proteins

International Aquatic Research

دوره 3، شماره 1، تیر 2011، صفحه 53-61   

نوع مقاله: Original research

نویسندگان

Soottawat Benjakul^{* 1}؛ Wonnop Visessanguan²؛ Tanong Aewsiri³؛ Munehiko Tanaka⁴؛ Mehdi Nikoo⁵

¹Prince Sungkala University, Thiland

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

چکیده

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. 

کلیدواژه‌ها

ATPase؛ Natural actomyosin؛ Prawn؛ Muscle؛ Autolysis؛ Proteinase