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- W2061741769 abstract "Invertase was purified from the cell extracts of the glutamic acid bacterium (Brevibacterium divaricatum) by ammonium sulfate fractionation, batch theatment with DEAE-cellulose, and column chromatographies on DEAE-cellulose, hydroxyapatite and Sephadex G-200. The purified enzyme was proved to be almost homogeneous by polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be 92,000 by both gel filtration and SDS-polyacrylamide gel electrophoresis methods. The optimum pH and temperature for the activity were 6.8 and 40°C. The enzyme was highly specific to sucrose as substrate, having only 10% as much activity toward raffinose as that toward sucrose, and being inert toward other disaccharides: maltose, trehalose, lactose, melibiose and cellobiose. The Km value for sucrose was 0.19 M. The enzyme required phosphate or arsenate ions for activity. Monovalent or divalent Cu ions and sulfhydryl reagents inhibited the enzyme." @default.
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- W2061741769 date "1986-01-01" @default.
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- W2061741769 title "Purification and properties of invertase from a glutamate-producing bacterium" @default.
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- W2061741769 doi "https://doi.org/10.1016/0385-6380(86)90120-2" @default.
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