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UCD Bionanoscience Research Group
Principal Investigator: Prof. Gil U. Lee
Research strands:
Down Stream Processing
We have introduced a new concept for the analysis and purification of the Bowman-Birk-Inhibitor (BBI), which is bioactive protein derived from soybean whey. By using a phage display technique we have identified a set of peptides that bind specifically to BBI for which no synthetic probes have been reported to date. These peptides have been covalent grafted onto superparamamagnetic beads and used for the rapid isolation of functional BBI from soybean protein using high gradient magnetophoretic separation (HGMS). The high affinity of the peptides and novel surface chemistry made it possible to purify BBI at > 90% purity from soybean whey in a single separation step in less than 60 minutes. The peptide probes and HGMS process described in this manuscript provide a new means for isolating BBI that overcomes the speed, cost, and throughput limitations imposed by traditional liquid chromatography. More broadly we believe that the peptide-HGMS approach can be applied to a range of bioactive compounds in foods. Thus, we believe this manuscript will be of particular interest to the food science and technology community that your journal serves.