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タイトル: | Inactivation of enzymes under high pressure : 1. Inactivation of salivary α-amylase under high pressure |
著者: | Kitamura, Kiyoshi |
著者名の別形: | キタムラ, キヨシ |
発行日: | 20-Dec-1965 |
出版者: | The Physico-Chemical Society of Japan |
誌名: | The Review of Physical Chemistry of Japan |
巻: | 35 |
号: | 1 |
開始ページ: | 44 |
終了ページ: | 49 |
抄録: | It has been found that α-amylase of human saliva is inactivated in aqueous solution by an application of high pressure above 5, 000kg/cm^2. The inactivation by high pressure follows first order kinetics, with respect to the enzyme concentration. The rate of inactivation is strongly accelerated by an increase in pressure corresponding -32 cm^3/mole of the activation volume at 30°. The activation enthalpy and the activation entropy are 8.2kcal./mole and -44 e. u. respectively, at 7500kg/cm^2 and pH 6.9. The rate of inactivation by pressure is also roughly proportional to hydrogen ion concentration in the solution at a pH between 4 and 10. These features of the inactivation by pressure of salivary α-amylase, resemble closely those of bacterial α-amylase. |
URI: | http://hdl.handle.net/2433/46862 |
出現コレクション: | Vol.35 No.1 |
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