@article{jfnr2014293,
author={{Gu, Chunmei and Song, Xinxiu and Zhao, Linlin and Pan, Shu and Qin, Guixin},
title={Purification and Characterization of Bowman-Birk Trypsin Inhibitor from Soybean},
journal={Journal of Food and Nutrition Research},
volume={2},
number={9},
pages={546--550},
year={2014},
url={http://pubs.sciepub.com/jfnr/2/9/3},
issn={2333-1240},
abstract={In this paper, crude extract of a Bowman-Birk trypsin inhibitor from soybean meal was firstly isolated by a combination of , thermal denaturation, isoelectric precipitation and acetone precipitation. Then this extract was purified by DE-52 ion exchange and affinity chromatography. The results showed that soybean Bowman-Birk trypsin inhibitor (SBBI) was purified to 50.07-fold with trypsin activity of 822.31 U¡¤mg-1. The purified SBBI gave a single protein band in SDS-PAGE electrophoresis. The accurate molecular mass of this inhibitor was determined to be 8837.46Da by MALDI-TOF. N-terminal sequence showed high homology with other serine proteinase inhibitors belonging to the Leguminosae family.},
doi={10.12691/jfnr-2-9-3}
publisher={Science and Education Publishing}
}