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Michaelis—Menten kinetic constants for the elimination of p353NP, BPA and TCS with laccase CLEAs unsupplemented with BSA at a pH of 5 and a temper- ature of 20°C* x 2 The values represent means of triplicate experiments + standard deviation.

Table 3 Michaelis—Menten kinetic constants for the elimination of p353NP, BPA and TCS with laccase CLEAs unsupplemented with BSA at a pH of 5 and a temper- ature of 20°C* x 2 The values represent means of triplicate experiments + standard deviation.

Related Figures (9)

Fig. 1. Laccase activity recovery after a 16-h precipitation at pH 7 and a tem- perature of 20°C using (M) buffer, (Ml) 55% (w/v) ammonium sulfate, (@ ) 79% (w/v) ethanol, (~ ) 67% (w/v) acetone or (Ml _) 100% (w/v) PEG as precipitant (mean of triplicates + standard deviation). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of the article.) The impact of the formation procedures on the activity of lac- case CLEAs was studied in two steps: (1) determining the best precipitant and its concentration and (2) determining the impact of cross-linker concentration (Schoevaart et al., 2004). Fig. 1
Fig. 1. Laccase activity recovery after a 16-h precipitation at pH 7 and a tem- perature of 20°C using (M) buffer, (Ml) 55% (w/v) ammonium sulfate, (@ ) 79% (w/v) ethanol, (~ ) 67% (w/v) acetone or (Ml _) 100% (w/v) PEG as precipitant (mean of triplicates + standard deviation). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of the article.) The impact of the formation procedures on the activity of lac- case CLEAs was studied in two steps: (1) determining the best precipitant and its concentration and (2) determining the impact of cross-linker concentration (Schoevaart et al., 2004). Fig. 1
Activity of laccase CLEAs and activity recovery using different amounts of BSA* x * The values represent means of triplicate experiments + standard deviation.
Activity of laccase CLEAs and activity recovery using different amounts of BSA* x * The values represent means of triplicate experiments + standard deviation.
Residual laccase activity (A/Ag) of laccase CLEAs after incubation with different denaturants* x ND, not determined. * The values represent means of triplicate experiments. Table 4
Residual laccase activity (A/Ag) of laccase CLEAs after incubation with different denaturants* x ND, not determined. * The values represent means of triplicate experiments. Table 4
* The values represent means of triplicate experiments + standard deviation. Michaelis-Menten kinetic constants of laccase CLEAs for the oxidation of ABTS? x
* The values represent means of triplicate experiments + standard deviation. Michaelis-Menten kinetic constants of laccase CLEAs for the oxidation of ABTS? x
Fig. 2. Residual activity (A/Ao) of laccase CLEAs after incubation with denaturants (mean of triplicates + standard deviation).
Fig. 2. Residual activity (A/Ao) of laccase CLEAs after incubation with denaturants (mean of triplicates + standard deviation).
* The values represent means of triplicate experiments. Kinetic inactivation parameters for laccase CLEAs and CLEAs formed with addition of BSA, subjected to a temperature of 40°C and a pH of 3* x
* The values represent means of triplicate experiments. Kinetic inactivation parameters for laccase CLEAs and CLEAs formed with addition of BSA, subjected to a temperature of 40°C and a pH of 3* x
Fig. 5. Continuous treatment of a 5mg1~! solution of (4) p353NP, (@) BPA and (Ml) TCS at pH 5 and at room temperature using 0.5 mg of laccase CLEAs in a fluidized bed reactor as a function of residence time. Fig. 4 shows the SEMs of CLEAs of laccase prepared without BSA and with 1 mg of BSA per unit of laccase activity. The BSA-free CLEAs were smaller than those made with the protein feeder, their length being between | and 5 wm although some
Fig. 5. Continuous treatment of a 5mg1~! solution of (4) p353NP, (@) BPA and (Ml) TCS at pH 5 and at room temperature using 0.5 mg of laccase CLEAs in a fluidized bed reactor as a function of residence time. Fig. 4 shows the SEMs of CLEAs of laccase prepared without BSA and with 1 mg of BSA per unit of laccase activity. The BSA-free CLEAs were smaller than those made with the protein feeder, their length being between | and 5 wm although some
Fig. 4. SEMs of laccase CLEAs and CLEAs formed with 1 mg BSA U~!: (A) CLEA (working distance = 11.4 mm, acceleration voltage = 5 kV); (B) CLEA (workit distance = 3.0 mm, acceleration voltage =3 kV); (C) CLEA-BSA 1 mg U7! (working distance = 11.4 mm, acceleration voltage =5 kV); (D) CLEA-BSA 1 mg U- (working distance = 3.0 mm, acceleration voltage = 3 kV).
Fig. 4. SEMs of laccase CLEAs and CLEAs formed with 1 mg BSA U~!: (A) CLEA (working distance = 11.4 mm, acceleration voltage = 5 kV); (B) CLEA (workit distance = 3.0 mm, acceleration voltage =3 kV); (C) CLEA-BSA 1 mg U7! (working distance = 11.4 mm, acceleration voltage =5 kV); (D) CLEA-BSA 1 mg U- (working distance = 3.0 mm, acceleration voltage = 3 kV).
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