title: [Purification and physico-chemical properties of Cryptococcus albidus 1001 alpha-L-rhamnosidase].
abstract: A scheme of isolation and purification of the enzyme with alpha-L-rhamnosidase activity from culture liquid Cryptococcus albidus 1001 has been developed. It included fractionation by ammonium sulfate and chromatography on TSK-gels Toyopearl HW-60, Fractogel TSK DEAE-650-s and Sepharose 6B. The enzyme was purified 42 times with the yield of 0.7 %. The enzyme preparation did not contain any glycosidase (except of beta-D-glucosidase) and proteolytic activity. Molecular mass of the alpha-L-rhamnosidase preparation by the data of Sepharose 6B gel-filtration was 50 kDa. The enzyme preparation was stable during 48 hours at 20 degrees C, its pH and thermal optimum were 4.0-5.0 and 60 degrees C, correspondingly.
mesh_terms: D000645:Ammonium Sulfate / Q000737:chemistry; D002850:Chromatography, Gel; D003454:Cryptococcus / Q000737:chemistry* / Q000201:enzymology; D004795:Enzyme Stability; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D012685:Sepharose; D013379:Substrate Specificity; D013696:Temperature; D001617:beta-Glucosidase / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D012685:Sepharose; D006026:Glycoside Hydrolases; D001617:beta-Glucosidase; C022525:alpha-L-rhamnosidase; D000645:Ammonium Sulfate