Purification and Properties of Invertase from a Glutamate-Producing Bacterium

概要

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Invertase was purified from the cell extracts of the glutamic acid bacterium(Brevibacterium divaricatum) by ammonium sulfate fractionation, batch treatment 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℃. 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 K_m 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.
社団法人日本生物工学会の論文
1986-08-25