Properties and stability of glycerophosphate oxidase isolated from a mutant strain of Aerococcus viridans.
The properties of microbial L-alpha-glycerophosphate oxidase (GPO) isolated from a mutant strain of Aerococcus viridans DBM 1509 were estimated. The stability at different temperatures and pH were detected. At 4 degrees C the enzyme lost activity during 15 d, at 20 degrees C and 30 degrees C GPO activity decreased during 30 and 25 h, respectively. The highest stability was measured at - 20 degrees C and pH 9. At 4 degrees C the stability was enhanced by the addition of 0.1 M EDTA or by lyophilization in the presence of dextrin. These conditions allow the prolongation of the low stability of microbial GPO which limited its use, and give the opportunity to increase the stability of other enzymes
MacKová
M
M
Department of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, Institute of Chemical Technology, Technická 3, 166 28 Prague, Czech Republic. martina.mackova@vscht.cz
Kost'Al
J
J
Demnerová
K
K
D003912:Dextrins; D004492:Edetic Acid; D004795:Enzyme Stability; D005612:Freeze Drying; D005993:Glycerolphosphate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009154:Mutation; D013289:Streptococcaceae / Q000201:enzymology* / Q000235:genetics; D013696:Temperature
D003912:Dextrins; D004492:Edetic Acid; D005993:Glycerolphosphate Dehydrogenase