Purification and Characterization of a 34-kDa Chitobiosidase from Aeromonas sp. GJ-18
2012
Jeong, H.C., Chonnam National University, Gwangju, Republic of Korea | Ju, W.T., Chonnam National University, Gwangju, Republic of Korea | Jo, K.H., Chonnam National University, Gwangju, Republic of Korea | Park, R.D., Chonnam National University, Gwangju, Republic of Korea
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℃, respectively. The enzyme was stable at pH 5-8 and 50℃ 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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