Production, partial purification and some properties of beta-galactosidase from Aspergillus carbonarius

Production of beta-galactosidase by Aspergillus carbonarius grown on deproteinized cheese whey as basal medium was optimized (cultivation period of 6 d, pH 4.5, cultivation temperature 30 degrees C). The enzyme was partially purified (52.9-fold with an overall yield of 45.3% and a final specific activity of 4588 mu kat/g protein. The optimum pH for the enzyme activity was pH 4.5. The enzyme is to some extent thermostable. Metal ions are not required for enzyme activity. The enzyme may be considered for prospective use in food industry.