Characterization of major protein phosphatases from selected species of Kluyveromyces. Comparison with protein phosphatases from Yarrowia lipolytica. |
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| Authors: | P Jolivet E Bergeron H Benyair J C Meunier |
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| Affiliation: | Institut national de la recherche agronomique, Institut national agronomique Paris-Grignon, Centre de Biotechnologie Agro-Industrielle, Thiverval-Grignon, France. jolivet@grignon.inra.fr |
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| Abstract: | Casein phosphatase activities have been identified in five yeast strains grown on Pi-deficient medium. Maximal endocellular activities appeared in the exponential phase. Exocellular phosphatases were significantly produced from Yarrowia lipolytica W-29 and Kluyveromyces marxianus, in the early stationary phase. Major phosphatases from K. marxianus were one heavy acid phosphatase composed of 64-67 kDa subunits, which could be secreted in the medium, and one type 2A protein phosphatase with an apparent molecular mass of 147 kDa and a 52 kDa catalytic subunit dissociated by 80% ethanol treatment. The characteristics of phosphatases purified from K. marxianus were compared with those previously purified from Y. lipolytica. |
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