Purification and characterization of dioscin-alpha-L-rhamnosidase from pig liver.
Dioscin-alpha-L-rhamnosidase was isolated, purified and partially characterized from pig liver. The maximum activity was reached at pH 7, 42 degrees C, 24 h, and 2% of substrate concentration. Fe3+ and Cu2+ inhibited the enzyme; the ion Ca2+ activated it. Mg2+ was an inhibitor at 100 mM, but it was an activator at 200 mM. Zn2+ could be a weak activator of the enzyme. The molecular weight of dioscin-alpha-L-rhamnosidase was about 47 kDa as determined by the method of SDS-polyacrylamide gel electrophoresis.
Qian
Srguleng
S
College of Food Science, Shenyang Agricultural University, Dongling-lu No. 120, Dongling-qu, Shenyang 110161, PR China.
Yu
Hongshan
H
Zhang
Chunzhi
C
Lu
Mingchun
M
Wang
Hongying
H
Jin
Fengxie
F
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002855:Chromatography, Thin Layer; D004144:Diosgenin / Q000031:analogs & derivatives / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D013552:Swine
C019357:dioscin; D006026:Glycoside Hydrolases; C504488:dioscin-alpha-L-rhamnosidase, pig; D004144:Diosgenin