Premium
Partial characterization of α‐mannosidase from Yarrowia lipolytica
Author(s) -
Vega Rosario,
Domínguez Angel
Publication year - 1988
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620280606
Subject(s) - yarrowia , catabolite repression , mannose , chemistry , mannosidase , yeast , biochemistry , enzyme , mutant , gene
An 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 K m 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.