20 β-Galactosidase

Publisher Summary This chapter presents information on the chemistry and enzymology of β-galactosidases. β-Galactosidases have been found in numerous microorganisms, animals, and plants. Tests for fermentation of lactose play an important role in diagnostic bacteriology of Enterobacteriaceae, so the occurrence of β-galactosidase in gram-negative rods has been extensively investigated. Enzymic activity is found in several hundred strains of Enterobacteriaceae, in strains of Pseudomonodaceae, Parvobacteriaceae, and Neisseriaceae. Among gram-positive bacteria Diplococcus pneumonia, Streptococcus lactis, Bacillus megaterium, Baccilus subtilis, and several Propionibacteria were found to produce β-galactosidase. The widespread occurrence of β-galactosidaee in mammalian organs is probably related to the multiple physiological functions of the enzyme. Most procedures for assaying β-galactosidase are based on the determination of the liberated aglycon. The most common substrates for assaying β-galactosidase, however, are chromogenic galactosides. The first of these substrates was β-nitro-phenyl β-D-galactoside. β-Galactosidase from E. coli is usually asayed in phosphate or tris buffers containing mercaptoethanol and optimal concentrations of sodium and divalent ions. Isolation and purification of β -galactosidase from E. coli is relatively easy. The enzyme represents up to 5% of the total proteins in some constitutive strains of E. coli . The large size and stability of the enzyme facilitate the procedure of isolation.

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