[Purification and physico-chemical properties of Eupenicillium erubescens alpha-L- rhamnosidase].
A scheme of isolation and purification of the enzyme with alpha-L-rhamnosidase activity 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 60 times with the yield of 0.5%. The enzyme preparation did not contain any glycosidase and proteolytic activity. Molecular mass of the alpha-L-rhamnosidase enzyme on the data of Sepharose 6B gel-filtration was 35 kDa. The enzyme preparation was stable during 48 hours at 20 degrees C, its pH- and thermal optimum were 5 and 60 degrees C, correspondingly.
E V
EV
Gudzenko
L D
LD
Varbanets
D000645:Ammonium Sulfate / Q000737:chemistry; D002847:Chromatography, Agarose; D003470:Culture Media; D004795:Enzyme Stability; D055324:Eupenicillium / Q000201:enzymology*; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013696:Temperature
D003470:Culture Media; D005656:Fungal Proteins; D006026:Glycoside Hydrolases; C022525:alpha-L-rhamnosidase; D000645:Ammonium Sulfate