A Novel Class of Protease from Choerospondias axillaris (Lapsi) Leaves

A novel protease from leaves of Choreospndias axillaris has been reported. C. axillaris , locally called Lapsi is dioceous, deciduous fruit - bearing large tree, having multiple daily uses. In an attempt to find method for determining sex of Lapsi at seedling stage , we stumbled upon a unique protease that has thwarted our effort to find sex - related protein. Thus protease is highly thermo - stable and acid resistant. Its preparation can be autoclaved without significant loss in activity. Its activity can be repeatedly precipitated by trichloroacetic acid. It possesses a Km value of 29 μM and V max 52.63 pmoles/min for bovine serum albumin as the substrate. It is catalytically so powerful that the level of soluble protein in leaf is below 20 μg per g dry weight. Lapsi leaf protease is an specific endopeptidase attacking peptide bonds that have phenylalanine, tyrosine, alanine and threonine / aspartic acid residues. ？ DOI: 10.3126/ijls.v3i0.2301