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Table 2 Comparison of kinetic parameters for three laccase substrates between two mutants and wild type of Klebsiella sp. 601 MCO

From: Engineering Klebsiella sp. 601 multicopper oxidase enhances the catalytic efficiency towards phenolic substrates

  Wild-type E106F α351-380M
DMP pH5.0 pH5.0 pH5.0
   Km (μM) 2,847 ± 30 1,176 ± 47 639 ± 17
   kcat (s-1) 37,800 ± 32 37,480 ± 886 79,913 ± 944
   kcat/Km (μM-1s-1) 13.27 31.87 125.06
ABTS pH3.0 pH3.6 pH3.6
   Km (μM) 539 ± 5.0 159 ± 1.0 284 ± 6.2
   kcat (s-1) 68,409 ± 342 32,595 ± 152 35,990 ± 704
   kcat/Km (μM-1s-1) 126.9 205.0 35,990 ± 704
SGZ pH6.8 pH6.8 pH6.8
   Km (μM) 11.67 ± 0.2 1.57 ± 0.02 1.46 ± 0.02
   kcat (s-1) 10.8 ± 0.1 2.43 ± 0.02 4.3 ± 0.05
   kcat/Km (μM-1s-1) 0.93 1.5 2.95
  1. All data obtained from three independent experiments are presented as the mean of Michaelis-Menten parameters with the standard deviation (SD). Detailed measurements and data analysis were performed as described in Experimental section.