Storage and affinity properties of Murraya koenigii trypsin inhibitor

The Murraya Koenigii trypsin inhibitor was found to be the major protein component of the seed extract. The quantity of protein was determined to be approximately 20% of total protein extracted by simple buffer extraction. During different stages of seed development after flowering, the protein concentrations were found to be 5.27, 5.5, 8.5, 18.8 and 20% in 7, 19, 25, 37 and 55 days, respectively. During seed germination, protein degradations were observed from 20% to 12, 7 and 2% in 13, 16 and 22 days, respectively. This inhibitor, earlier purified using ion-exchange and gel filtration chromatography, was purified in single step by affinity column, using Cibacron blue 3GA, with substantial increase in yield. In partial internal sequencing by MALDI-TOF-TOF, six peptides of varying length, totalling 98 amino acid residues, exhibited similarities to the sequences from protease inhibitors, storage proteins and homeodomain-like proteins.