Research Article

Insight into the Hydrolytic Selectivity of β-Glucosidase to Enhance the Contents of Desired Active Phytochemicals in Medicinal Plants

Table 2

Relative specific activities and enzyme kinetics of β-glucosidase from Lactobaillus antri (rBGLa).

ChemicalsRelative activity ()Kinetic parameter
kcat (s-1)Km (mM)kcat/Km (mM-1 s-1)

pNPG100 ± 1407 ± 71.84 ± 0.07221 ± 9

pNPG + 0.1mM cellobiose57.3 ± 1.5432 ± 324.40 ± 0.5798.1 ± 14.7

pNPGr0.00123 ± 0.000060.213 ± 0.005102 ± 60.00209 ± 0.00012

Liquiritin37.1 ± 0.3---

Geniposide2.20 ± 0.04---

Baicalin0.0261 ± 0.0002---

Glycyrrhizin0.000190 ± 0.000103---

Hesperidin0.0199 ± 0.0005---

Neohesperidin0.00120 ± 0.00004---

Naringin0.000866 ± 0.000090---

pNPG, p-nitrophenyl β--glucopyranoside; pNPGr, p-nitrophenyl β--glucuronide.
For the measurement of relative activities, 1 mM substrates were reacted with 100 μg/mL rBGLa (pNPG, pNPGr, baicalin, glycyrrhizin, hesperidin, and naringin) and 0.1 μg/mL rBGLa (liquiritin and geniposide).