Studies of some biochemical and physicochemical properties of an inducible form of extracellular laccase from the basidiomyceteCoriolus hirsutus |
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Authors: | O N Gorbatova E V Stepanova O V Koroleva |
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Institution: | (1) Mendeleev University of Chemical Technology, Miusskayapl. 9, 125190 Moscow, Russia;(2) Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, 117071 Moscow, Russia |
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Abstract: | An inducible form of extracellular laccase (EC 1.14.18.1) was isolated from the basidiomyceteCoriolus hirsutus. The induction was performed with 0.11 μM syringaldazine, a substrate of laccase. The inducible form of the enzyme consisted
of two isoforms, laccase II and laccase 12, whose molecular weights were 69 ±2 and 67 ±2 kDa, respectively. The isoelectric
points of these isoenzymes were found to be 3.5 and 4.2, respectively. The optimum pH range for both laccases was 4.4–4.6,
and the optimum temperature was 50°C. The thermal stability of these isoenzymes was examined, andK
m values for the substrates syringaldazine and pyrocatechol were determined. Our biochemical and physicochemical studies demonstrated
that inducible laccase isoforms differed from constitutive forms in molecular weight, IEP,K
m, and thermal stability. However, their optimum pH ranges and temperatures were identical. |
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