Publication informationFood Chemistry, 134 (4): 1831-1838Publisher Elsevier Item record/more information http://hdl.handle.net/10197/8385 Publisher's statementThis is the author's version of a work that was accepted for publication in Food Chemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Food Chemistry (VOL 134, ISSUE 4, (2012) AbstractSoybean proteins offer exceptional promise in the area of cancer prevention and treatment.Specifically, soybean Bowman-Birk inhibitor (BBI) has the ability to suppress carcinogenesis in vivo, which has been attributed to BBI's serine protease activity, made possible by the presence of two distinct binding sites for trypsin and chymotrypsin. The lack of molecular tools for the isolation and identification of this protein has made it difficult to work with, limiting progress as a significant candidate in the treatment of cancer. This study has successfully identified a set of novel synthetic peptides targeting the Bowman-Birk inhibitor, using a phage display screening approach, and has demonstrated the ability to isolate BBI from crude mixtures. These peptide probes have been covalently immobilized on superparamagnetic (SPM) microbeads to allow for high gradient magnetic purification from crude soy whey mixtures in a single step. Our ultimate goal is for the described probe to be utilised to facilitate the isolation of this therapeutically relevant protein for low cost, scalable analysis and production of BBI.

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