Purification and Characterization of a Glucoamylase from Humicola grisea.

@article{Campos1995PurificationAC,
  title={Purification and Characterization of a Glucoamylase from Humicola grisea.},
  author={Laura Campos and Carlos Roberto F{\'e}lix},
  journal={Applied and environmental microbiology},
  year={1995},
  volume={61 6},
  pages={2436-8}
}
A thermostable extracellular glucoamylase from the thermophilic fungus Humicola grisea was purified to homogeneity. Its molecular mass and isoelectric point were 74 kDa and 8.4, respectively. The enzyme contained 5% carbohydrate, showed maximal activities at pH 6.0 and 60(deg)C, and was stable at 55(deg)C and pH 6.0 for 2 h. The K(infm) of soluble starch hydrolysis at 50(deg)C and pH 6.0 was 0.14 mg/ml. The purified enzyme was remarkably insensitive to glucose.