Purification and characterization of Kunitz trypsin inhibitor from soybean

DOI

10.2991/iceesd-17.2017.119How to use a DOI?

Keywords

soybean; Kunitz trypisin inhibitor; purification; characterization

Abstract

In this paper, a Kunitz trypsin inhibitor from soybean meal was isolated to apparent homogeneity by a combination of phosphoric acid extraction, heat treatment, ammonium sulfate precipitation, ion exchange chromatography, affinity chromatography and gel filtration. The results showed that the specific activity of 4733 Uúmg-1 and purification fold of 72.39 were obtained. The purified Kunitz trypsin inhibitor appeared a single protein band in SDS-PAGE electrophoresis. The accurate molecular mass of this inhibitor was determined as 22907.51Da by MALDI-TOF. Partial amino acid sequence of the purified protein from Edman degration showed a high degree of homology with various members of the Kunitz-inhibitor family.

Copyright

© 2017, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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TY  - CONF
AU  - Chunmei Gu
AU  - Shujun Li
AU  - Xinxiu Song
PY  - 2017/04
DA  - 2017/04
TI  - Purification and characterization of Kunitz trypsin inhibitor from soybean
BT  - Proceedings of the 2017 6th International Conference on Energy, Environment and Sustainable Development (ICEESD 2017)
PB  - Atlantis Press
SP  - 659
EP  - 666
SN  - 2352-5401
UR  - https://doi.org/10.2991/iceesd-17.2017.119
DO  - 10.2991/iceesd-17.2017.119
ID  - Gu2017/04
ER  -