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Purification and Characterization of a Protease from Korean Pear (Pyrus serotina L.) as Meat Tenderizer
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 Title & Authors
Purification and Characterization of a Protease from Korean Pear (Pyrus serotina L.) as Meat Tenderizer
Guan, Hao-Li; Mandal, P.K.; Lim, Hee-Kyong; Baatartsogt, Oyungerel; Lee, Chi-Ho; Jeon, Gwang-Joo; Choe, Il-Shin; Choi, Kang-Duk;
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This study was conducted for the isolation, purification, and characterization of a protease from Korean pear, to see its proteolytic activity on chicken actomyosin and to find the optimum pH and temperature of activity on chicken actomyosin. The protease was isolated from crude extract of Korean pear by ammonium sulfate precipitation. Further purification was done by DEAE-Sepharose ion-exchange chromatography, Mono-Q and Mini-Q column chromatography. The purified enzyme gave a single protein band on SDS polyacrylamide gel electrophoresis and the molecular weight was found to be 38 kDa. The specific activity of purified enzyme was 34,907 unit/mg with 25 fold purification and the yield was 2%. The purified enzyme incubated with chicken actomyosin showed high activity. The optimum pH and temperature for enzyme activity on chicken actomyosin were 6.5 and , respectively. A protease was purified from Korean pear for the first time and characterized. It was found to be promising for meat tenderization.
Korean pear protease;characterization;proteolytic activity;chicken actomyosin;tenderizer;
 Cited by
과숙청과물 연화제를 첨가한 소시지의 물성 연구,곽지혜;백무열;김병용;

산업식품공학, 2011. vol.15. 2, pp.116-121
양념 소갈비의 조리과정에서의 물리화학적 특성 평가,홍상필;김영호;이남혁;허영욱;

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