Isolation of Bowman-Birk-Inhibitor from soybean extracts using novel peptide probes and high gradient magnetic separation.

Abstract

Soybean proteins offer exceptional promise in the area of cancer prevention and treatment. Specifically, Bowman-Birk Inhibitor (BBI) has the ability to suppress carcinogenesis in vivo, which has been attributed to BBI's inhibition of serine protease (trypsin and chymotrypsin) activity. The lack of molecular probes for the isolation of this protein has made it difficult to work with, limiting its progress as a significant candidate in the treatment of cancer. This study has successfully identified a set of novel synthetic peptides targeting the BBI, and has demonstrated the ability to bind BBI in vitro. One of those probes has been covalently immobilised on superparamagnetic microbeads to allow the isolation of BBI from soy whey mixtures in a single step. Our ultimate goal is the use of the described synthetic probe to facilitate the isolation of this potentially therapeutic protein for low cost, scalable analysis and production of BBI.

• Authors: Conor Fields, Paul Mallee, Julien Muzard, Gil U Lee
• Journal: Food chemistry (Food Chem) Vol. 134 Issue 4 Pg. 1831-8 (Oct 15 2012) ISSN: 1873-7072 [Electronic] England
• PMID: 23442627 (Publication Type: Evaluation Study, Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2012 Elsevier Ltd. All rights reserved.

Chemical References

• Molecular Probes
• Peptide Library
• Peptides
• Trypsin Inhibitor, Bowman-Birk Soybean

Topics

• Amino Acid Sequence
• Magnetics (methods)
• Molecular Probe Techniques
• Molecular Probes (chemical synthesis, chemistry, genetics)
• Molecular Sequence Data
• Peptide Library
• Peptides (chemical synthesis, chemistry, genetics)
• Soybeans (chemistry)
• Trypsin Inhibitor, Bowman-Birk Soybean (chemistry, genetics, isolation & purification)