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. 1965 Dec;97(3):715–722. doi: 10.1042/bj0970715

Intracellular trehalase of a hybrid yeast

G Avigad 1, Ofra Ziv 1, Edna Neufeld 1
PMCID: PMC1264751  PMID: 5881661

Abstract

1. The trehalase found in an extract prepared from a yeast strain that cannot ferment trehalose was studied and characterized. The enzyme is highly specific for trehalose with Km 1·02×10−2m, and an optimum pH of 6·9. 2. It is inhibited by glucose and by trehalose 6-phosphate, 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 thiol-binding reagents. 5. The possible role of this enzyme in the trehalose-dissimilation patterns in the yeast cell was evaluated.

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Selected References

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