Characterization of a thermostable extracellular beta-galactosidase from a thermophilic fungus Rhizomucor sp.

@article{Shaikh1999CharacterizationOA,
  title={Characterization of a thermostable extracellular beta-galactosidase from a thermophilic fungus Rhizomucor sp.},
  author={Shahid Ahmed Shaikh and Jayant Malhar Khire and Mohamad I Khan},
  journal={Biochimica et biophysica acta},
  year={1999},
  volume={1472 1-2},
  pages={314-22}
}
An extracellular beta-galactosidase from a thermophilic fungus Rhizomucor sp. has been purified to homogeneity by successive DEAE cellulose chromatography followed by gel filtration on Sephacryl S-300. The native molecular mass of the enzyme is 250,000 and it is composed of two identical subunits with molecular mass of 120,000. It is an acidic protein with a pI of 4.2. Purified beta-galactosidase is a glycoprotein and contains 8% neutral sugar. The optimum pH and temperature for enzyme activity… CONTINUE READING