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1,4-dioxan
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complete inhibition at 50% or above
chloroform
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1:1 buffer-chloroform, completely stable for 2 h
diethylene triamine
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amongst 42 solvents tested, significant deactivation is observed only in the presence of diethylene triamine (less than 50% of activity retains after 6 h incubation), which is probably due to the stripping-off of the crucial bound-water monolayer from the enzyme molecule essential for its activity
glycer0l
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slight loss of activity at 10% v/v
isoamyl alcohol
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slight loss of activity at 10% v/v
isopropyl alcohol
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slight loss of activity at 10% v/v
N,N-dimethylformamide
81.2% activity remaining after 14 days in 25%
n-heptane
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slight loss of activity at 10% v/v
n-hexane
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slight loss of activity at 10% v/v
tert-Butanol
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slight loss of activity at 10% v/v
additional information
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1% (v/v) Triton X-100 and 8 M urea have little or no influence on the strength of cuticle laccase activity
1-propanol
9% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
1-propanol
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9% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
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Acetone
10% v/v, 10°C, 1 h, 100% of activity remains
Acetone
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the laccase retains about 60% of its activity in the presence of 5% (v/v) acetone
Acetone
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the laccase retains about 60% of its activity in the presence of 5% (v/v) acetone
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Acetone
rLac1 retains less than 20% activity in 50% v/v acetone after a 3 h incubation at 25°C
Acetone
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rLac1 retains less than 20% activity in 50% v/v acetone after a 3 h incubation at 25°C
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Acetone
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complete inhibition at 50% or above
Acetone
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retains high degree of activity
Acetone
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slight loss of activity at 10% v/v
Acetone
Sporothrix carnis
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 27% loss of activity
Acetone
Sporothrix carnis CPF-05
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 27% loss of activity
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Acetone
MK290990.1
20%, 75.9% residual activity after 16 h of preincubation
Acetone
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10% (v/v), the enzyme retains more than 89.68% activity
Acetone
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10% (v/v), the enzyme retains more than 89.68% activity
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acetonitril
77.5% activity remaining after 14 days in 25%
acetonitril
rLac1 retains less than 20% activity in 50% v/v acetonitril after a 3 h incubation at 25°C
acetonitrile
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10% (v/v), 15 min, 91.8% activity compared to control
acetonitrile
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10% (v/v), 15 min, 91.8% activity compared to control
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acetonitrile
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
acetonitrile
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
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acetonitrile
30% (v/v), 70% loss of activity, recombinant enzyme
acetonitrile
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30% (v/v), 70% loss of activity, recombinant enzyme
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acetonitrile
25% (v/v), 4 h, 25°C, no loss of activity
acetonitrile
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25% (v/v), 4 h, 25°C, no loss of activity
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acetonitrile
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the laccase retains about 75% of its activity in the presence of 5% (v/v) acetonitrile
acetonitrile
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the laccase retains about 75% of its activity in the presence of 5% (v/v) acetonitrile
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acetonitrile
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complete inhibition at 50% or above
acetonitrile
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retains high degree of activity
acetonitrile
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 39% loss of activity
acetonitrile
Sporothrix carnis CPF-05
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 39% loss of activity
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acetonitrile
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10% (v/v), the enzyme retains more than 93.38% activity
acetonitrile
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10% (v/v), the enzyme retains more than 93.38% activity
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acetonitrile
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stabilizes the concentrated or lyophilized enzyme at 1%
dimethyl formamide
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
dimethyl formamide
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
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dimethyl sulfoxide
10% v/v, 10°C, 1 h, 72% of activity remains
dimethyl sulfoxide
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
dimethyl sulfoxide
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
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dimethyl sulfoxide
30% (v/v), 65% loss of activity, recombinant enzyme
dimethyl sulfoxide
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30% (v/v), 65% loss of activity, recombinant enzyme
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dimethyl sulfoxide
55.8% activity remaining after 14 days in 25%
dimethyl sulfoxide
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
dimethyl sulfoxide
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25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
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dimethyl sulfoxide
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 46% loss of activity
dimethylformamide
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10% (v/v), 15 min, 58.8% activity compared to control
dimethylformamide
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10% (v/v), 15 min, 58.8% activity compared to control
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dimethylformamide
25% (v/v),4 h, 25°C, no loss of activity
dimethylformamide
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25% (v/v),4 h, 25°C, no loss of activity
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dimethylformamide
rLac1 retains more than 80% activity in 50% v/v dimethylformamide after a 3 h incubation at 25°C
dimethylformamide
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rLac1 retains more than 80% activity in 50% v/v dimethylformamide after a 3 h incubation at 25°C
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dimethylformamide
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
dimethylformamide
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25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
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dimethylformamide
Sporothrix carnis
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 36% loss of activity
dimethylformamide
Sporothrix carnis CPF-05
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 36% loss of activity
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DMSO
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10% (v/v), 15 min, 42.3% activity compared to control
DMSO
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10% (v/v), 15 min, 42.3% activity compared to control
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DMSO
25% (v/v), 4 h, 25°C, no loss of activity
DMSO
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25% (v/v), 4 h, 25°C, no loss of activity
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DMSO
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the laccase retains about 70% of its activity in the presence of 5% (v/v) DMSO
DMSO
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the laccase retains about 70% of its activity in the presence of 5% (v/v) DMSO
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DMSO
rLac1 retains more than 80% activity in 50% v/v DMSO after a 3 h incubation at 25°C
DMSO
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rLac1 retains more than 80% activity in 50% v/v DMSO after a 3 h incubation at 25°C
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Ethanol
10% v/v, 10°C, 1 h, 84% of activity remains
Ethanol
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10% (v/v), 15 min, 96.36% activity compared to control
Ethanol
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10% (v/v), 15 min, 96.36% activity compared to control
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Ethanol
25% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
Ethanol
30% (v/v), 65% loss of activity, recombinant enzyme
Ethanol
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25% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
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Ethanol
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30% (v/v), 65% loss of activity, recombinant enzyme
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Ethanol
25% (v/v), 4 h, 25°C, no loss of activity
Ethanol
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25% (v/v), 4 h, 25°C, no loss of activity
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Ethanol
84.8% activity remaining after 14 days in 25%
Ethanol
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the laccase retains about 75% of its activity in the presence of 5% (v/v) ethanol
Ethanol
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the laccase retains about 75% of its activity in the presence of 5% (v/v) ethanol
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Ethanol
rLac1 retains more than 80% activity in 50% v/v ethanol after a 3 h incubation at 25°C
Ethanol
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rLac1 retains more than 80% activity in 50% v/v ethanol after a 3 h incubation at 25°C
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Ethanol
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
Ethanol
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25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
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Ethanol
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slight loss of activity at 10% v/v
Ethanol
Sporothrix carnis
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 34% loss of activity
Ethanol
Sporothrix carnis CPF-05
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 34% loss of activity
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Ethanol
MK290990.1
20%, 82.3% residual activity after 16 h of preincubation
Ethanol
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10% (v/v), the enzyme retains more than 92.55% activity. At 50% (v/v), the enzyme loses about 85% activity after 1 h
Ethanol
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10% (v/v), the enzyme retains more than 92.55% activity. At 50% (v/v), the enzyme loses about 85% activity after 1 h
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Methanol
10% v/v, 10°C, 1 h, 95% of activity remains
Methanol
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10% (v/v), 15 min, 82.5% activity compared to control
Methanol
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10% (v/v), 15 min, 82.5% activity compared to control
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Methanol
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
Methanol
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presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
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Methanol
18% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
Methanol
30% (v/v), 50% loss of activity, recombinant enzyme
Methanol
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18% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
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Methanol
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30% (v/v), 50% loss of activity, recombinant enzyme
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Methanol
25% (v/v), 4 h, 25°C, no loss of activity
Methanol
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25% (v/v), 4 h, 25°C, no loss of activity
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Methanol
74.6% activity remaining after 14 days in 25%
Methanol
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the laccase retains more than 75-80% of its activity in the presence of 5% (v/v) methanol
Methanol
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the laccase retains more than 75-80% of its activity in the presence of 5% (v/v) methanol
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Methanol
rLac1 retains more than 80% activity in 50% v/v methanol after a 3 h incubation at 25°C
Methanol
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rLac1 retains more than 80% activity in 50% v/v methanol after a 3 h incubation at 25°C
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Methanol
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
Methanol
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25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
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Methanol
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complete inhibition at 50% or above
Methanol
-
slight loss of activity at 10% v/v
Methanol
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 29% loss of activity
Methanol
Sporothrix carnis CPF-05
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50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 29% loss of activity
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Methanol
MK290990.1
20%, 85.12% residual activity after 16 h of preincubation
Methanol
-
10% (v/v), the enzyme retains more than 94% activity
Methanol
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10% (v/v), the enzyme retains more than 94% activity
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propanol
MK290990.1
20%, 79.1% residual activity after 16 h of preincubation
propanol
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10% (v/v), the enzyme retains more than 92.89% activity
propanol
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10% (v/v), the enzyme retains more than 92.89% activity
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