All Title Author
Keywords Abstract

Investigation of isolation conditions and ion-exchange purification of protein coagulation components from common bean seed

DOI: 10.2298/apt0738003a

Keywords: Natural coagulant , common bean seed , extraction and purification , proteins , coagulation activity

Full-Text   Cite this paper   Add to My Lib


Investigation of an extraction procedure of protein coagulants from common bean seed regarding concentration of NaCl and pH was performed. High values of protein concentration and coagulation activity in crude extract (9.19 g/l and 23.9%, respectively) were obtained when the extraction was performed using 0.5 mol/l NaCl and water as solvent, which represents an advantage for economic and environmental reasons. Crude extract of common bean seed was purified by precipitation at two different percentages of (NH4)2SO4 saturation, followed by batch ion-exchange chromatography. The highest obtained coagulation activity, 45%, was determined in fraction that was eluated at 1.75 mol/l NaCl from resin loaded with proteins precipitated upon 80-100% (NH4)2SO4 saturation. High values of coagulation activity showed by some eluates suggest their application as natural coagulant for water purification. .


comments powered by Disqus