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Cloning, production and secretion of β-galactosidase inAcetobacter pasteurianus

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Abstract

The gene coding for β-galactosidase fromEscherichia coli was cloned into plasmid pACT71 containing the replicon from plasmid pAC1 fromAcetobacter pasteurianus. E. coli MC4100,E. coli JM105,E. coli LE392.23 andA. pasteurianus 3614 were transformed with the recombinant plasmid pACB815. Cells were cultivated in LB, YPG and M media supplemented with glucose, glycerol, lactose or ethanol and β-galactosidase activity was detected in the cells and in the cultivation medium. The best substrate for production of β-galactosidase was lactose. To release β-galactosidase fromA. pasteurianus cells amino acids were added to the cultivation medium. The highest secretory activity was achieved using 1.5% glycine after 36 h of cultivation in the M medium.

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Grones, J., Bencová, K. Cloning, production and secretion of β-galactosidase inAcetobacter pasteurianus . Folia Microbiol 39, 99–104 (1994). https://doi.org/10.1007/BF02906802

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  • DOI: https://doi.org/10.1007/BF02906802

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