Abstract
A fungal strain isolated from rotten banana and identified as Aspergillus alliaceus was found capable of producing thermostable extracellular β-galactosidase enzyme. Optimum cultural conditions for β-galactosidase production by A. alliaceus were as follows: pH 4.5; temperature, 30 °C; inoculum age, 25 h; and fermentation time, 144 h. Optimum temperature, time, and pH for enzyme substrate reaction were found to be 45 °C, 20 min, and 7.2, respectively, for crude and partially purified enzyme. For immobilized enzyme–substrate reaction, these three variable, temperature, time, and pH were optimized at 50 °C, 40 min, and 7.2, respectively. Glucose was found to inhibit the enzyme activity. The K m values of partially purified and immobilized enzymes were 170 and 210 mM, respectively. Immobilized enzyme retained 43 % of the β-galactosidase activity of partially purified enzyme. There was no significant loss of activity on storage of immobilized beads at 4 °C for 28 days. Immobilized enzyme retained 90 % of the initial activity after being used four times.
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The authors would like to thank Jadavpur University for financial support for the entire research work.
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Sen, S., Ray, L. & Chattopadhyay, P. Production, Purification, Immobilization, and Characterization of a Thermostable β-Galactosidase from Aspergillus alliaceus . Appl Biochem Biotechnol 167, 1938–1953 (2012). https://doi.org/10.1007/s12010-012-9732-6
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DOI: https://doi.org/10.1007/s12010-012-9732-6