β-galactosidase (EC 126.96.36.199) is important in the formation of a medicinal plant Artemisia judaica (al-ba’atharan) aroma. The crude plant extracts of Artemisia judaica were used to characterize the enzyme in the term of pH, temperature, enzyme kinetic and effects of some heavy metals on its activity. The enzyme activity was measured by its ability to hydrolyze the substrate 2-nitrophenyl β-D-galactopyranoside (ONPG). The enzyme activity was reached maximum at 50°C and at pH 6.0. The Km and Vmax values of the enzyme were 3.6 mM and 1.67 μmol/min, respectively. Uncompetitive inhibition was observed in presence of Hg+2, Fe+3 and Zn+2 for the enzyme β-galactosidase in the crude extract through the decrease in the Km and Vmax values. Pb+2 and Cu+2 were found to act as a noncompetitive inhibitors on the enzyme β-galactosidase in the crude extract due to increase in the Km values and decrease in Vmax values. The study showed that Hg+2 was the most potent inhibitor while Cu+2 exhibited the least inhibition degree on β-galactosidase activity in the Artemisia judaica. These finding indicated that the enzyme β-galactosidase in the crude leaves extract of Artemisia judaica can be used in industrial and medical applications.
Omar M. Atrooz,
Mohammad H. Abukhalil,
Ibrahim M. AlRawashdeh,
Characterization of β-galactosidase in the Crude Plant Extract of Artemisia judaica L. in Presence and Absence of Some Heavy Metals, American Journal of Life Sciences.
Vol. 4, No. 5,
2016, pp. 99-105.
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