ｐＨ変化を伴う酵素反応における活性の一測定法　ＩＩ　　中性，および弱アルカリ性プロテイナーゼのエステラーーゼ活性の一測定法

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  • The Estimation of the Esterolytic Activity of Neutral and Slightly Alkaline Protease by Using Acid-base Indicators
  • チュウセイ オヨビ ジャクアルカリセイ プロテアーゼ ノ エステラーゼ カッセ

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Esterase activities of trypsin, chymotrypsin, papain, subtilisin BPN' andAchromobacter lyticus protease-I toward TAME, BAEE and ATEE were estimated by using acidbase indicators.<br> The principle of this method was based on the measurement of the absorbance changes of acid-base indicators, i, e., phenol red (PR), or neutral red (NR), caused by the increase of hydrogen ion liberated from above substrates during the esterase action.<br> The reaction mixture consisted of 8.3 μ/ml of PR in 15 to 20mM Tris-HCl buffer, pH 8.0 (PR-T method), or 6.7 μg/ml of NR in 10mM phosphate buffer, pH 7.0_??_7.9 (NR-P method), together with 1.85mM to 20mM of substrates. The absorbance changes were monitored at 560 nm (PR-T method) or at 530 nm (NR-P method) at 30°C during the enzyme action for 5min.<br> The Km of subtilisin BPN' and Achromobacter lyticus protease-I for BAEE obtained by PR-T method were 10.0mM and 18.1mM, respectively. The Km and Kcat of papain for BAEE by NR-P method were 20.0mM and 10.1 sec-1. These values were well accorded with the reported values which were estimated by pH-stat method.

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