[Production, partial purification and characterization of methamidophos-degrading enzyme from methylotroph WB-1].
After cultivation for 20 h in the inorganic salt medium with methamidophos as sole carbon and nitrogen source, Methylotroph WB-1 could produce methamidophos-degrading enzyme in larger amounts. The enzyme was partially purified by sonication disruption, Tween-20 extraction, heat treatment(9 min at 60 degrees C), DEAE-cellulose 32 and CM-cellulose32 chromatography with 22.8 times purification and 78.8% recovery. Activity staining showed single violate band corresponding to that of protein staining. Optimum pH of the enzyme was 9.0; poor substrate specificity was showed. It was strongly inhibited by Hg2+, Mn2+ and Cu2+, but not by Co2+ and Zn2+; it also exhibited poor stability.
Chao
Y
Y
Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071.
Zhao
Y
Y
Liu
B
B
Wang
Y
Y
D000333:Aeromonas / Q000201:enzymology* / Q000378:metabolism; D001673:Biodegradation, Environmental; D002848:Chromatography, DEAE-Cellulose; D004795:Enzyme Stability; D004798:Enzymes / Q000302:isolation & purification* / Q000378:metabolism; D009946:Organothiophosphorus Compounds / Q000378:metabolism*; D013379:Substrate Specificity
D004798:Enzymes; D009946:Organothiophosphorus Compounds; C014655:methamidophos