Purification and Characterization of Protease from Chickpeas | ||||
| Journal of Bioscience and Applied Research | ||||
| Volume 11, Issue 1, March 2025, Page 64-73 PDF (1.06 MB) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/jbaar.2025.417818 | ||||
 View on SCiNiTO | ||||
| Authors | ||||
Ayat Adnan Abbas  ; Mohammed Omar Abel latif
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| 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 | ||||
| chickpea; protease; purification; characterization; HPLC; DPPH; FTIR | ||||
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