ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Beta-galactosidase (Beta-D-galactosidegalactohydrolase, EC 3.2.1.23) of Streptococcus cremoris H was partially purified by ammonium sulfate fractionation. Only 10% of the protein was recovered as enzyme protein and more than 50% of the enzyme in the crude extract was lost. A 2.6-fold purification only was achieved. The enzyme was most active at 65°C and recorded an optimum pH at 7.0. Km and Vmax with ortho-nitrophenyl beta-D galactopyranoside as the substrate were recorded as 0.384 mM and 12.6 μmoles/mg protein/min. Manganese ions activated the enzyme. The enzyme was strongly inhibited by Hg++, Ca++, Ni++, and Ag+ as well as parachloromercuribenoate.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1981.tb14554.x
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