Characterization of Choreospondias axillaris (Lapsi) fruit protease

A catalytically powerful protease from Choreospondias axillaris (Lapsi) fruit has been reported . C. axillaris (Lapsi) is dioecious, deciduous fruit bearing tree. The protease extracted from the pulp of the fruit is highly thermo stable, autoclavable and extreme acidic and basic pH resistant. Its activity was retained even after multiple trichloro acetic acid (TCA) precipitation. The proteolytic activity of the protease increased linearly up to protein concentration of 62.28μg. It possesses a Km value of 13.09 μM and Vmax 15.87 pmoles/min for bovine serum albumin (BSA) as a substrate. Sodium Dodecyl Sulphate (SDS) activated the proteolytic activity. DOI: 10.3126/ijls.v3i0.2386 Int J Life Sci Vol.3 2009 p.19-26