Stereochemistry of the Hydrolysis of Trehalose by the Enzyme Trehalase Prepared from the Flesh Fly Sarcophaga barbata

Open Access
Publisher Website
Google Scholar
Abstract
1 The enzyme trehalase was prepared from whole flesh flies, Sarcophaga barbata. 2 The rate of mutorotation of glucose released by the enzyme was compared with that of α-d-glucose, β-d-glucose and an equimolar mixture of the two. 3 Derivatives of the glucose released by the enzyme were prepared and analysed by gas chromatography for anomeric composition. 4 The enzyme was incubated with trehalose in a medium enriched with H218O and the glucose was analysed by gas chromatography/mass spectrometry. 5 It was found that an equimolar mixture of α-d-glucose and β-d-glucose is formed on hydrolysis of trehalose by trehalase and 18O is incorporated into β-d-glucose. 6 These results indicate that there is an inversion of configuration at C-1 of trehalose on hydrolysis and that the hydrolysis proceeds by a bimolecular nucleophilic substitution mechanism.