Abstract
Production of β-galactosidase byAspergillus carbonarius grown on deproteinized cheese whey as basal medium was optimized (cultivation period of 6 d, pH 4.5, cultivation temperature 30 °C). The enzyme was partially purified (52.9-fold with an overall yield of 45.3 % and a final specific activity of 4588 µkat/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.
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El-Gindy, A. Production, partial purification and some properties of β-galactosidase fromAspergillus carbonarius . Folia Microbiol 48, 581–584 (2003). https://doi.org/10.1007/BF02993462
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DOI: https://doi.org/10.1007/BF02993462