Purification and Characterization of Protease from Chickpeas

Document Type : Original Article

Authors

Environmental Biotechnology Department, Biotechnology Research Center, Al-Nahrain University, Baghdad, Iraq

Abstract

The main aim of the present study was to isolate, purify, and characterize a protease from chickpeas. A 0.1 M phosphate buffer at pH 8.0 was used for protease extraction. Following the rinsing of unattached proteins with a (pH 8.0) 20 mM Tris-2 mM CaCl2 solution and subsequent size exclusion filtering using Sephadex G-50 in the same buffer, the required protein was subsequently eluted using 0.5 M NaCl. The protease was subjected to further optimization by precipitating ammonium sulphate at a 75% concentration. Protease exhibited activity throughout the pH range of 6.0 to 8.0, it was entirely active at 35°C. Subsequently, DPPH, FTIR, and HPLC analysis was applied.

Keywords

Journal of Bioscience and Applied Research
Volume 11, Issue 1 - Serial Number 1
January- February- March
March 2025
Pages 64-73

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