Phagedependent overproduction of β-galactosidase Escherichia coli and working out its purification
DOI:
https://doi.org/10.7124/bc.0004C4Abstract
The phagedependent method of obtaining of β-galactosidase (EC 3.2.1.23) E. coli has been worked out. The yield was up 700 U of enzyme activity per ml of cultural fluid. Accumulation of enzyme in cultural medium has permitted to use membrane method for preliminary purification of β-galactosidase. Concentrated and partially purified preparation of β-galactosidase has been purified by ligand-affinity chromatography. Pure preparation of β-galactosidase has characterized by high purity and nativeness. The process of obtaining and purification of β-galactosidase were made in pilot scale.References
Kaul R, D'Souza SF, Nadkarni GB. Hydrolysis of milk lactose by immobilized beta-galactosidase-hen egg white powder. Biotechnol Bioeng. 1984;26(8):901-4.
Houts Sandra S. Lactose intolerance. Food Technol. 1988. 42(3):110-3.
Gibbons I, Skold C, Rowley GL, Ullman EF. Homogeneous enzyme immunoassay for proteins employing beta-galactosidase. Anal Biochem. 1980;102(1):167-70.
Freytag JW. Affinity column mediated immunoenzymometric assay. In: Enzyme-mediated immunoassay. Eds. TT Ngo, HM Lemhoff. Plenum Press New York 1985 277-298.
Li XL, Robbins JW Jr, Taylor KB. The production of recombinant beta-galactosidase in Escherichia coli in yeast extract enriched medium. J Ind Microbiol. 1990;5(2-3):85-93.
Kane JF, Hartley DL. Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotechnol. 1988;6(5):95–101.
AS. USSR N 1593232 Al. A method of producing ?-galactosidase. VA Kordyum, SI Chernykh, IYu Slavchenko, VG Korobko. 15.05.1990.
Griffith KL, Wolf RE Jr. Measuring beta-galactosidase activity in bacteria: cell growth, permeabilization, and enzyme assays in 96-well arrays. Biochem Biophys Res Commun. 2002;290(1):397-402. Erratum in: Biochem Biophys Res Commun 2002 Mar 22;292(1):292.
Affinity chromatography: a practical approach : Ed PD Dean, WS Johnson, FA Middle, IRL Press, Oxford, Washington, 1985, 215 p.