The kinetics of the action of purified β-glucuronosidase upon mentholglucuronate were studied. The results are summarised as follows:-
1. The optimal pH of this enzyme action lies at 5.0-5.2, under the buffering with acetate mixture.
2. The reaction velocity of this enzyme action proceeds mono-molecular.
3. The temperature coefficient shows the average value of 2.66 in the range of 30°-45°C.
Then the heat of activation is 36340 cal.
4. Irradiation of ultraviolet ray produces a strong inhibiting effect.
5. The addition of neutral salt promotes the enzyme action in a remarkable manner.
6. The sodium salts of oxydicarbonic acids such as malic-, tartaric-, and citric acids exhibit a powerful inhibiting effect, while those of lactic-, acetic-, propionic-, and butyric acids rather promote. The plausible explanation for this phenomenon was sug-gested.
Thanks are due to Prof. K. Kodama and Prof. H. Masa-mune for their criticisms and encouragement.
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