Purification and characterization of Kunitz trypsin inhibitor from soybean
Chunmei Gu, Shujun Li, Xinxiu Song
Available Online April 2017.
- https://doi.org/10.2991/iceesd-17.2017.119How to use a DOI?
- soybean; Kunitz trypisin inhibitor; purification; characterization
- 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.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
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 - https://doi.org/10.2991/iceesd-17.2017.119 ID - Gu2017/04 ER -