Activities of Protease, Tyrosinase and Myosin ATPase in <I>Euphausia superba</I>
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In the previous paper the authors have reported on the nutritional values for rats, amino acid composition and artificial digestibility of extracted <I>Euphausia superba (E. superba)</I> protein concentrate compared with whole egg protein.<BR>In this experiments the authors have investigated with reference to the protease and tyrosinase activity that is presumed to be closely related to autolysis and discoloration of <I>E. superba.</I> Furthermore, myosin ATPase activity was measured by considering with the fish jelly products of <I>E. superba.</I> Sample of <I>E. superba</I> frozen on board immediately after catching was obtained from Antarctic Ocean and frozen fresh prawn and shrimp were used as a control. Protease activity was measured with liberated amino acid by Lowry method. Tyrosinase activity was measured with oxygen up-take using manometer by Keilin Mann method. Myosin ATPase activity was determined with liberated phosphorous by Fiske Subbarow method.<BR>The following results were obtained.<BR>(1) Protease activity of <I>E. superba</I> was recognized to be of much higher against prawn and shrimp protease activity, but optimum pH and temperature of <I>E. superba</I> shrimp protease showed the same values of pH 8.0 and 40°C.<BR>(2) Tyrosinase activity of prawn and shrimp using catechol as substrate showed higher tendency than <I>E. superba</I> tyrosinase activity. And more, optimum pH and temperature of <I>E. superba</I> or shrimp tyrosinase was pH 7.5 and 25°C.<BR>(3) The values of myosin ATPase activity on <I>E. superba</I> was confirmed to be clearly different in comparison to prawn and shrimp myosin ATPase activity. The optimum pH and temperature of <I>E. superba</I> or shrimp myosin ATPase was recognized to be pH 6.0 and 20°C.
- 公益社団法人 日本栄養・食糧学会の論文
公益社団法人 日本栄養・食糧学会 | 論文
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