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 s tability 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 act ivity decreased during 30 and 25 h, respectively. The highest stability was measured at 20 degrees C and pH9. At 4 degrees C the stability was enhance d by the addition of 0.1 M EDTA or by lyophilization in the presence of dex trin. These conditions allow the prolongation of the low stability of micro bial GPO which limited its use, and give the opportunity to increase the st ability of other enzymes.