Evidence is obtained for the existence of two different localizations of trehalase (Ξ±,Ξ±-trehalose glucohydrolase, EC 3.2.1.28) in Phycomyces spores: one inside the cell, and one in the periplasmic region. The latter enzyme is sensitive to 0.1 mol l(-1) HCl treatment and its activity can be regulated
Trehalase activity in dormant and activated spores ofPhycomyces blakesleeanus
β Scribed by J. A. Assche; A. R. Carlier; Helena I. Dekeersmaeker
- Publisher
- Springer-Verlag
- Year
- 1972
- Tongue
- English
- Weight
- 360 KB
- Volume
- 103
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
Heat treatment of Phycomyces sporangiospores, which breaks dormancy, causes a very rapid 10- to 15fold increase in trehalase activity; soon after the heat shock the enzyme activity decays. This phenomenon can be repeated several times by repeating the heat shocks. Prolonging the heat treatment over the minimum required time delays the decay of enzyme activity. Cycloheximide does not prevent the rise in enzyme activity. It is suggested that heat treatment converts temporarily an inactive form of trehalase into an active one. Optimal enzyme activity is obtained at pH 7.5 and the enzyme requires metal ions for maximal activity. The possible role of trehalase in the spore-activation process is discussed.
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