Nuniek Herdyastuti, Sari Edi Cahyaningrum, Tri Joko Raharjo
Chitinase enzyme is produced by the bacterial Pseudomonas sp which has been isolated from mud fields. The enzyme was precipitated with ammonium sulphate 0-50 % demonstrated by increasing up to 1.3 fold in purity compared to before fractionation. The molecular mass of the purified chitinase was 26.1 and 29 kDa, estimated by a sodium dodecyl sulfate Polyacrylamide gel electrophoresis and was confirmed by activity staining with Calcofluor white M2R. Chitinase was optimally active at pH of 5.0 at 35 °C. The enzyme showed stability of activity at pH range 3-5 and temperature of 40 °C, an apparent KM value of 1.51 mg/mL and Vmais 0.35 μmL/mL hour. Among the metals, ions, the Cu2+ and Fe2+ completely inhibited the activity enzyme but activated in presence of is Mn2+ in 10 mM concentration.
Department of Chemistry, Surabaya State University, Jl. Ketintang Surabaya, Indonesia; Department of Chemistry, Gadjah Mada University, Sekip Utara Yogyakarta, Indonesia
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