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  • Title: Purification and characterization of chondroitinase ABC from Acinetobacter sp. C26.
    Author: Zhu C, Zhang J, Zhang J, Jiang Y, Shen Z, Guan H, Jiang X.
    Journal: Int J Biol Macromol; 2017 Feb; 95():80-86. PubMed ID: 27769932.
    Abstract:
    An extracellular chondroitinase ABC (ChSase ABC, EC 4.2.2.4) produced by cultivating Acinetobacter sp. C26, was purified to homogeneity from the supernatant by ammonium sulfate fractionation, Q-Sepharose Fast Flow and Sephadex G-100 chromatography. The 76kDa enzyme was purified 48.09-fold to homogeneity with specific activity of 348.64U/mg, Using the chondroitin sulfate A (CS-A) as substrate, the maximal reaction rate (Vmax) and Michaelis-Menten constant (Km) of ChSase ABC were found to be 10.471μmol/min/ml and 0.105mg/ml, respectively. The enzyme showed the highest activity at the optimal conditions of pH 6.0 and 42 ∘C, respectively. This enzyme was stable at pH 5-10, 5-9 and 5-7 at 4°C, 37°C and 42°C, respectively. Investigation about thermal stability of ChSase ABC displayed that it was stable at 37°C. ChSase ABC activity was increased in presence of Na+, K+, Mn2+, 1,10-phenanthrolin and strongly inhibited by Cu2+, Hg2+, Al3+and SDS. These properties suggested that ChSase ABC from Acinetobacter sp. C26 bring promising prospects in medical and industry applications.
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