ONPG is a colorimetric and spectrophotometric substrate for detection of β-galactosidase activity.
性状
Solid
体外研究(In Vitro)
The enzyme displays high hydrolysis ability for ONPG (100%) and moderate activity for its natural substrate lactose (25.7%). However, the hydrolysis ability of the enzyme towards all other chromogenic nitrophenyl analogues is very weak, indicating that Gal308 is a β-galactosidase with narrow substrate specificity. To investigate the kinetic parameters of recombinant enzyme, the Michaelis-Menten constants (Km), turnover numbers (kcat), and catalytic efficiencies (kcat/Km) of Gal308 for ONPG and lactose are determined. The kcat and Km values are 464.7±7.8 s and 2.7±0.3 mM for ONPG, and 264.2±2.1 s and 7.1±0.8 mM for lactose, respectively. The kcat/Km value of the enzyme for ONPG (172.1 smM) is 4.6-fold higher than that for lactose (37.2 smM), which clearly demonstrated that the catalytic effi
运输条件
Room temperature in continental US; may vary elsewhere.
储存方式
Powder -20°C 3 years;4°C 2 years
参考文献
[1]. Zhang X, et al. Metagenomic approach for the isolation of a thermostable β-galactosidase with high tolerance of galactose and glucose from soil samples of Turpan Basin. BMC Microbiol. 2013 Oct 24;13:237. doi: 10.1186/1471-2180-13-237.
溶解度数据
In Vitro: H2O : 8.33 mg/mL (27.65 mM; ultrasonic and warming and heat to 60°C)配制储备液