Abstract

K. S. Chandrashekharaiah

DOI : http://dx.doi.org/10.13005/ojc/290329

The trypsin inhibitor has been purified to apparent homogeneity from the seeds of Mucuna pruriens employing ammonium sulfate fractionation, cation exchange chromatography on CMcellulose and gel-permeation chromatography on Sephadex G-100. The purified Mucuna pruriens trypsin inhibitor (MPTI) showed a specific inhibitor activity of 474.66, fold purity of 99.51 and the yield obtained was 22.08%. The homogeneity of the purified preparation was confirmed by PAGE, IEF and SDS–PAGE. The molecular weight determined by gel-permeation chromatography and SDS–PAGE were 12 and 11.6 kDa respectively. The pI of MPTI was found to be 5.6 ± 0.05. MPTI was found to be stable at all temperatures lying between 0 and 90 ºC and pH 2.0 – 10 and hence exhibited high stability. The MPTI was inhibited both trypsin and chymotrypsin showing the double headed nature. Antifungal studies showed inhibitory activity of MPTI against Aspergillus niger and Trichoderma viridae.

Mucuna pruriens;trypsin inhibitor;purification;characterization;antifungal Properties

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