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A simplified method for the purification of an intrinsically disordered coagulant protein from defatted Moringa oleifera seeds

Paper ID Volume ID Publish Year Pages File Format Full-Text
34155 45005 2016 7 PDF Available
Title
A simplified method for the purification of an intrinsically disordered coagulant protein from defatted Moringa oleifera seeds
Abstract

•A coagulant protein from M. oleifera seed extract was purified to a purity of 94%.•Purified MOCP was capable to aggregate bentonite colloids in aqueous solutions.•MOCP remained stable at 121 °C and 1.5 bar for at least 15 min.•MOCP is proposed to be an intrinsic disordered protein.

Coagulant proteins from Moringa oleifera (MO) seeds were successfully purified by removing seed oil followed by a protein salting out method at 40% (NH4)2SO4 combined with subsequent dialysis and heat treatment. A microtiter plate-based coagulation activity assay was then performed using colloidal bentonite solution and alum as positive control. The results show an oil recovery of 40 ± 2% while the water-soluble protein fraction in the defatted MO seed was 12.5 ± 0.5 mg/g or 4.4% of the total seed protein content. Heating the desalted protein fraction to 121 °C helped to obtain a 94% pure protein of approximately 7 kDa. Computational analyses support the hypothesis that the coagulating MO protein is an intrinsically disordered protein, providing reason for its stability at extreme temperatures (121 °C). The purified, thermo-stable coagulating protein retained its coagulating activity paving the way to economically produce a sterile natural coagulant from MO seeds.

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Keywords
Moringa oleifera; Coagulation activity assay; Protein purification; Heat treatment; Intrinsically disordered protein
First Page Preview
A simplified method for the purification of an intrinsically disordered coagulant protein from defatted Moringa oleifera seeds
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 51, Issue 8, August 2016, Pages 1085–1091
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering