Dextransucrase from Leuconostoc mesenteroides NRRL B-512F: Characterization of the Enzyme Bound to Sephadex Gel

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A dextransucrase with high affinity for Sephadex G-100 gel was purified from Leuconostoc mesenteroides NRRL B-512F. The purified enzyme was very similar in its subunit molecular weight and properties to those of the main component of dextransucrase from B-512F. The stability of the enzyme was significantly increased by glycerol (33%) and bovine serum albumin (0.1%). Addition of exogenous dextran stimulated the sucrase activity (reducing sugar production) 1.3-fold, and the transferase activity (dextran synthesis) was increased 9.6-fold. Thus, the exogenous dextran clearly improved the efficiency of polymer synthesis. A micro-determination of enzyme activity by a fluorescent reagent BEC (borate ethanolamine complex) allowed for kinetic examination at lower substrate concentrations, which gave biphasic double reciprocal plots for the substrate sucrose.