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Purification and characterization of a 34-kDa chitobiosidase from Aeromonas sp. GJ-18

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  • Biochemistry
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Abstract

Chitobiosidase was purified and characterized from Aeromonas sp. GJ-18 by ammonium sulfate precipitation, anion-exchange chromatography, and gel filtration chromatography. The purified enzyme has a molecular weight of 34 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme showed an optimum pH and temperature of 6.0 and 30–50°C, respectively. The enzyme was stable at pH 5–8 and 50°C and was completely inhibited in the presence of 10 mM Zn2+ ions. The enzyme could efficiently hydrolyze colloidal chitin into N,N′- diacetylchitobiose as the major product, indicating that the purified enzyme is a chitobiosidase. When colloidal chitin was used as the substrate, the K m and V max of this enzyme were established as 3.45 mg/mL and 2.91 μmol/min, respectively.

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Correspondence to Ro Dong Park.

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Jeong, H.C., Ju, WT., Jo, KH. et al. Purification and characterization of a 34-kDa chitobiosidase from Aeromonas sp. GJ-18. J Korean Soc Appl Biol Chem 55, 7–12 (2012). https://doi.org/10.1007/s13765-012-0002-7

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  • DOI: https://doi.org/10.1007/s13765-012-0002-7

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