Structure of the beta-galactosidase gene from Thermus sp. strain T2: expression in Escherichia coli and purification in a single step of an active fusion protein

Article Abstract:

A study was conducted to characterize the nucleotide sequence of the beta-galactosidase gene from Thermus sp. strain T2. Recombinant DNA methods were carried out using standard protocols while beta-galactosidase assays were determined with o-nitrophenyl-beta-D-galactopyranoside in Z buffer. Results indicated that beta-galactosidases produced in Escherichia coli still retain its catalytic features and thermostability.

Genetic aspects, Escherichia coli, Nucleotide sequence, Base sequence, Bacterial genetics, Galactose

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Overproduction of Thermus sp. strain T2 beta-galactosidase in Escherichia coli and preparation by using tailor-made metal chelate supports

Article Abstract:

Research demonstrates the production of a chimeric beta-galactosidase bearing a poly-His tag from Thermus sp. strain T2 in Escherichia coli. The recombinant protein retains the wild-type enzyme biochemical properties. Furthermore, low-activated cobalt- or nickel-iminodiacetic acid support provides as one-point adsorption point to facilitate purification of the enzyme.

Spain, All Other Miscellaneous Chemical Product and Preparation Manufacturing, Chelating Agents, Chemical preparations, not elsewhere classified, Usage, Physiological aspects, Microbial enzymes, Protein synthesis, Gene expression, Protein biosynthesis, Recombinant proteins, Beta galactosidases

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Genetic modification of the penicillin G acylase surface to improve its reversible immobilization on ionic exchangers

Article Abstract:

The mutant form of the enzyme penicillin G acylase is found to increase adsorption on anionic exchangers. The reversible immobilization of the enzyme is also improved by gathering eight novel glutamic residues through enzyme surface via mutagenesis.

Mutagenesis, Penicillin G, Immobilization

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