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자료유형
학술대회자료
저자정보
Lee, Eun-Jung (Div. of Food Material Processing Technology, Korea Food Research Institute) Kim, Yun-Ji (Div. of Food Material Processing Technology, Korea Food Research Institute) Lee, Nam-Hyouck (Div. of Food Material Processing Technology, Korea Food Research Institute) Yamamoto, Katsuhiro (Depart. of Food Science, Rakuno Gakuen University)
저널정보
한국축산식품학회 한국축산식품학회 학술발표초록집 한국축산식품학회 2004년도 정기총회 및 제33차 춘계 학술대회
발행연도
2004.1
수록면
198 - 201 (4page)

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To investigate hydrostatic pressure (HP) effect on myofibrillar protein (Mf) extracted from bovine Semitendinosus muscle, Ca- and Mg-ATPase activities to evaluate denaturation of myosin and actin, and soluble protein contents were observed. In Mf treated with 100 MPa for 5 min was not observed denaturation of myosin and actin. In Mf treated with 200 MPa for 5 min, denaturation of myosin and actin were observed but inactivation rate was low (0.0136 $min^{-1}$). Inactivation rate of myosin and actin was dramatically increased above 300 MPa treatment. However denaturation of myosin and actin was not that critical with duration time. By increasing pressure size, the amount of myosin and actin in soluble protein eluted in 20 mM potassium phosphate buffer (pH 7.0) containing 0.6 M NaCl were decreased. SDS-PAGE of soluble protein released from Mf suspension in 0.1 M NaCl buffer (pH 7.0) showed that low molecular weight proteins (15${\sim}$36 KDa) were released by HP treatment above 200 MPa. From the results, denaturation of myosin and actin, and release of light molecule proteins of Mf were observed by HP treatment over 200 MPa.

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