Биохимия и аналитическая биохимия

Абстрактный

Biochemical Characterization of Protease Isolated from Different Parts of Choerospondias axillaris (Lapsi)

Shrawan Kumar Upadhyay, Rubin Thapa Magar and Chandan Jung Thapa

Proteases were isolated from leaf, bark and root of Choerospondias axillaris, locally called Lapsi. Choerospondias axillaris is a dioecous, deciduous fruit bearing plant with multiple daily uses. The protease was extracted with 0.1 M phosphate buffer of pH 7 and then precipitated successively with TCA and ammonium sulfate. The protease from leaf showed maximum activity at pH 9, temperature at 20°C. While, bark protease showed optimum pH 5 and temperature 60°C. In case of root the optimum pH was 10 and the optimum temperature 35°C. The optimum time of incubation leaf, bark and root was 15 minute. The bell shaped curve was obtained for the effect of enzyme conc. with optimum enzyme conc. 50 μg for leaf, 30 μg for bark and 50 μg for root. The Km and Vmax value of leaf were 5.61 μM and 185.18 pmol/ min, Km and Vmax value of bark were 2.36 μM and 82.64 pmol/min. While for root, the Km and Vmax values were 1.53 μM and 52.91 pmol/min.