Purification and characterization of an intracellular α-glucosidase with high transglycosylation activity from A. niger M-1.

@article{Zhang2011PurificationAC,
  title={Purification and characterization of an intracellular α-glucosidase with high transglycosylation activity from A. niger M-1.},
  author={Yun-kai Zhang and Wei Li and Kong-yang Wu and Gui-guang Chen and Zhi-qun Liang},
  journal={Preparative biochemistry & biotechnology},
  year={2011},
  volume={41 2},
  pages={201-17}
}
An intracellular α-glucosidase with high transglycosylation activity was purified from a mutant strain of Aspergillus niger M-1 by sequential chromatography using a DEAE-cellulose 52 column, a DEAE-Sepharose CL-6B column, and a Sephadex G-100 column. The molecular mass of the purified enzyme was determined to be 116 kD with no subunits and a pI of 5.23. Maximal α-glucosidase activity occurred at pH 6.0 and 50°C. The N-terminal amino acid sequences were identified as N-SVPGTEYVV-. The presence… CONTINUE READING