Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II.

@article{Liu1993PurificationCA,
  title={Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II.},
  author={X Liu and Sayaka Maeda and Zheng Hu and Toshihiro Aiuchi and Ken-ichi Nakaya and Yasuyuki Kurihara},
  journal={European journal of biochemistry},
  year={1993},
  volume={211 1-2},
  pages={281-7}
}
A new sweet protein, named mabinlin II, was extracted with 0.5 M NaCl solution from the seeds of Capparis masaikai Lévl. and purified by ammonium sulfate fractionation, carboxymethylcellulose-Sepharose ion-exchange chromatography and gel filtration. The sweetness of mabinlin II was unchanged by at least 48 h incubation at nearly boiling temperature. Purified mabinlin II thus obtained gave a single band having a molecular mass of 14 kDa on SDS/PAGE. In the presence of dithiothreitol, mabinlin II… CONTINUE READING