Intracellular trehalase of a hybrid XXXX .

@entity7970 @entity1432 @entity375 @entity413 @entity45021
1. The trehalase found in an extract prepared from a @entity375 that cannot ferment @entity7970 was studied and characterized. The enzyme is highly specific for @entity7970 with K(m) 1.02x10(-2)m, and an optimum pH of 6.9. 2. It is inhibited by @entity413 and by @entity45021 , and does not facilitate any significant transglucosylations. 3. pK values 7.7 and 5.8 were detected for the groups associated with binding of the non-ionized substrate to the enzyme. 4. The trehalase was found to be highly labile and was inhibited by @entity1432 -binding reagents. 5. The possible role of this enzyme in the @entity7970 -dissimilation patterns in the @entity375 cell was evaluated.
