Abstract

AbstractAn exo‐α‐mannosidase (E.C. 3.2.1.24) was characterized in the yeast form of Yarrowia lipolytica. The enzyme located in a crude particulate fraction of the cell extract is under catabolite repression, has an optimum pH of 6.0, a Km of 0.27 mM with p‐nitrophenyl‐α‐D‐mannopyranoside and is partially inhibited by D‐mannose.The enzyme is not affected by ethylenediaminotetraacetic acid, several cations (only Zn++ increased its activity in a 25%) or sulphydryl reagents and can be partially solubilized by treatment with digitonine.

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