Vigna unguiculata Trypsin Inhibitor: A Protein with Versatile Biological Applications

摘要

Background: Trypsin Inhibitors are one of the most promising and investigated subject fortheir role in pharmacognostical and pharmacological studies.Aim: The paper describes purification and characterization of trypsin inhibitor obtained from blackeyedcowpea (Vigna unguiculata).Methods: The purification procedure of Vigna unguiculata trypsin inhibitor (VUTI) includes homogenizationfollowed by ammonium sulphate precipitation. The protein thus precipitated was further dialysedand purified by ion exchange chromatography and gel permeation chromatography. The molecularweight was determined by SDS-PAGE. The protein thus purified was characterized biochemicallyto demonstrate curative potential as strong antioxidant, anti-inflammatory and antimicrobialagent.Results: The 15 kDa VUTI obtained showed IC50 values 490 μg/ml compared to standard which was254μg/ml in 1, 1-diphenyl-2-picrylhydrazyl (DPPH) assay. Also, the highest ferric reducing antioxidantpower (FRAP) results confirmed the highest FRAP value of 0.405 mM at 1000 μg/ml and thelowest value of 0.113 mM at 100 μg/ml which were quite comparable to ascorbic acid (standard).Anti-inflammatory activity of VUTI was depicted by the method of inhibition of albumin denaturationwhere, VUTI showed high IC50 value of 696.46 μg/ml. Also, VUTI showed good antibacterial potentialby inhibiting all tested bacterial strains with maximum inhibition against Bacillus subtilis(99.62%) and minimum against Staphylococcus aureus (34.62%). The results were quite comparablewith standard drug ampicillin (5 mg/ml). Unfortunately, VUTI failed to show any activity againstfungi.Conclusion: Thus, the results obtained depict that VUTI additionally be a wonderful candidate for developmentof novel antibacterial drugs, and it can also be used to reduce the deletorious effects of freeradicals.