Steric course of the hydrolysis of alpha,alpha-trehalose and alpha-D-glucosyl fluoride catalyzed by pig kidney trehalase.

Article abstract of DOI:10.1016/0008-6215(89)85013-X

We are unable to confirm the report of Labat et al.3 that pig kidney trehalase hydrolyzes alpha,alpha-trehalose to form solely alpha-D-glucose. Highly purified trehalase from pig renal cortex was found, in reactions monitored by 1H-n.m.r. spectra, to hydrolyze alpha,alpha-trehalose with the formation of both alpha- and beta-D-glucose. That the beta anomer constitutes the enzymically mobilized glucosyl residue is indicated by the further finding that beta-D-glucose is the product formed on hydrolysis of alpha-D-glucosyl fluoride by the enzyme. Present results show the stereochemical behavior of pig kidney trehalase in hydrolyzing alpha,alpha-trehalose to be indistinguishable from that reported by ourselves and others for trehalase preparations from a range of biological sources including rabbit renal cortex.