RT Journal Article SR Electronic(1) A1 Vasileva-Tonkova, Evgenija S. A1 Galabova, Danka N. A1 Balasheva, Marija A. A1 Sotirova, Anna V.YR 1993 T1 Purification and Partial Characterization of Acid Phosphatase from Candida Lipolytica JF Microbiology, VO 139 IS 3 SP 479 OP 483 DO https://doi.org/10.1099/00221287-139-3-479 PB Microbiology Society, SN 1465-2080, AB Non-specific acid phosphatase from Candida lipolytica cells was purified 111-fold by chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 and Sepharose 4B. The enzyme is a glycoprotein containing 67% neutral sugars. The molecular mass of the highly purified acid phosphatase was found to be approximately 95 kDa by both SDS-PAGE and gel filtration. The pH and temperature optima were 5·8 and 55 °C, respectively. The enzyme was stable at pH values between 3·5 and 5·5 and at temperatures up to 60 °C. The purified phosphatase had a K m value of 364 mm for p-nitrophenyl phosphate and showed broad substrate specificity., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-139-3-479