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4-nitroacetanilide + H2O
?
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butyrate + H2O
?
-
-
-
-
?
acetanilide + H2O
?
-
-
-
-
?
benzylcarbamate + H2O
CO2 + NH3 + benzoate
butyl carbamate + H2O
CO2 + NH3 + butanol
-
-
-
-
?
butyramide + H2O
?
-
-
-
-
?
ethyl carbamate + H2O
CO2 + NH3 + ethanol
-
-
-
-
?
ethyl N-phenylcarbamate + H2O
CO2 + aniline + ethanol
-
-
-
-
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
hexamethylene dicarbamic acid dibutyl ester + H2O
?
-
-
product identification and quantification, overview
-
?
L-alanine-4-nitroanilide + H2O
?
-
-
-
-
?
methyl carbamate + H2O
methanol + CO2 + NH3
methylcarbamate + H2O
CO2 + NH3 + methanol
methylene bisphenyl dicarbamic acid dibutyl ester + H2O
?
-
-
product identification and quantification, overview
-
?
n-butylcarbamate + H2O
CO2 + NH3 + n-butanol
phenyl acetamide + H2O
?
-
-
-
-
?
phenylcarbamate + H2O
CO2 + NH3 + phenol
tert-butylcarbamate + H2O
CO2 + NH3 + tert-butanol
toluene-2,4-dicarbamic acid dibutyl ester + H2O
toluene diamine + ?
-
-
product identification and quantification, overview
-
?
urethane + H2O
ethanol + CO2 + NH3
additional information
?
-
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
acetamide + H2O
?
-
78% of the activity with ethylcarbamate
-
-
?
acetamide + H2O
?
-
880% of the activity with ethylcarbamate
-
-
?
acetamide + H2O
?
-
-
-
-
?
acetamide + H2O
?
-
-
-
-
?
benzamide + H2O
?
-
30% of the activity with ethylcarbamate
-
-
?
benzamide + H2O
?
-
680% of the activity with ethylcarbamate
-
-
?
benzamide + H2O
?
-
-
-
-
?
benzamide + H2O
?
-
-
-
-
?
benzylcarbamate + H2O
CO2 + NH3 + benzoate
-
132% of the activity with ethylcarbamate
-
-
?
benzylcarbamate + H2O
CO2 + NH3 + benzoate
-
148% of the activity with ethylcarbamate
-
-
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
equimolar amounts of ammonia and ethanol
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
equimolar amounts of ammonia and ethanol, noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
equimolar amounts of ammonia and ethanol, noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
enzyme may play an important role in detoxification of urethane
equimolar amounts of ammonia and ethanol, noncarcinogenic compounds
?
methyl carbamate + H2O
methanol + CO2 + NH3
-
20% of the activity with ethyl carbamate, i.e. urethane
-
-
?
methyl carbamate + H2O
methanol + CO2 + NH3
-
20% of the activity with ethyl carbamate, i.e. urethane
-
-
?
methylcarbamate + H2O
CO2 + NH3 + methanol
-
64% of the activity with ethylcarbamate
-
-
?
methylcarbamate + H2O
CO2 + NH3 + methanol
-
64% of the activity with ethylcarbamate
-
-
?
n-butylcarbamate + H2O
CO2 + NH3 + n-butanol
-
192% of the activity with ethylcarbamate
-
-
?
n-butylcarbamate + H2O
CO2 + NH3 + n-butanol
-
224% of the activity with ethylcarbamate
-
-
?
n-butyramide + H2O
?
-
93% of the activity with ethylcarbamate
-
-
?
n-butyramide + H2O
?
-
1000% of the activity with ethylcarbamate
-
-
?
phenylcarbamate + H2O
CO2 + NH3 + phenol
-
197% of the activity with ethylcarbamate
-
-
?
phenylcarbamate + H2O
CO2 + NH3 + phenol
-
96% of the activity with ethylcarbamate
-
-
?
tert-butylcarbamate + H2O
CO2 + NH3 + tert-butanol
-
118% of the activity with ethylcarbamate
-
-
?
tert-butylcarbamate + H2O
CO2 + NH3 + tert-butanol
-
24.4% of the activity with ethylcarbamate
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
hydrolyzes carbamoyl ester derivatives more rapidly than amide derivatives
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl acetate
-
-
?
additional information
?
-
-
no activity with urea, methylurea, ethylurea, n-butylurea, tert-butylurea, phenylurea
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
no activity with urea, methylurea, ethylurea, n-butylurea, tert-butylurea, phenylurea
-
-
?
additional information
?
-
-
no activity with glycinamide, N-alkyl ureas, N-allylurea, ethyl esters of organic acids, ethyl acetate, ethyl benzoate, diethyl carbonate, phenylphosphorodiamide, phenylthiophosphorodiamide, N-benzoylphosphoric triamide
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase activity
-
-
?
additional information
?
-
-
high-sensitive electrochemical determination of ethyl carbamate using urethanase and glutamate dehydrogenase modified electrode, with high selectivity during biorecognition between enzymes and the targets, overview
-
-
?
additional information
?
-
-
high-sensitive electrochemical determination of ethyl carbamate using urethanase and glutamate dehydrogenase modified electrode, with high selectivity during biorecognition between enzymes and the targets, overview
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
high-sensitive electrochemical determination of ethyl carbamate using urethanase and glutamate dehydrogenase modified electrode, with high selectivity during biorecognition between enzymes and the targets, overview
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with L-leucine-4-nitroanilide, methyl benzoate, and ethyl benzoate
-
-
?
additional information
?
-
-
the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with L-leucine-4-nitroanilide, methyl benzoate, and ethyl benzoate
-
-
?
additional information
?
-
-
no or poor activity with gamma-aminobutyric acid, glutamic acid, and glycine
-
-
?
additional information
?
-
-
a highly sensitive spectrophotometric method for ethyl carbamate (EC) determination is established through glutamate dehydrogenase/urethanase cascade reactions and the corresponding change in NADH concentration. The absorbance at 340 nm is linearly related to the EC concentration within the range of 300-5000 nM, with a low detection limit of 9.28 nM. Method optimization. The absorbance declines slowly at either pH 4.5 or pH 8.0, which is around the optimal pH of one of the enzymes. But the absorbance decreases with the fastest rate at pH 6.0
-
-
?
additional information
?
-
-
a highly sensitive spectrophotometric method for ethyl carbamate (EC) determination is established through glutamate dehydrogenase/urethanase cascade reactions and the corresponding change in NADH concentration. The absorbance at 340 nm is linearly related to the EC concentration within the range of 300-5000 nM, with a low detection limit of 9.28 nM. Method optimization. The absorbance declines slowly at either pH 4.5 or pH 8.0, which is around the optimal pH of one of the enzymes. But the absorbance decreases with the fastest rate at pH 6.0
-
-
?
additional information
?
-
-
no or poor activity with gamma-aminobutyric acid, glutamic acid, and glycine
-
-
?
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ethylcarbamate + H2O
CO2 + NH3 + ethanol
hexamethylene dicarbamic acid dibutyl ester + H2O
?
-
-
-
-
?
methylene bisphenyl dicarbamic acid dibutyl ester + H2O
?
-
-
-
-
?
toluene-2,4-dicarbamic acid dibutyl ester + H2O
toluene diamine + ?
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
additional information
?
-
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
urethane, potentially carcinogenic, mutagenic and teratogenic to human
equimolar amounts of ammonia and ethanol, noncarcinogenic compounds
?
ethylcarbamate + H2O
CO2 + NH3 + ethanol
-
enzyme may play an important role in detoxification of urethane
equimolar amounts of ammonia and ethanol, noncarcinogenic compounds
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
urethane + H2O
ethanol + CO2 + NH3
-
-
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
-
-
?
additional information
?
-
-
the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
-
-
?
additional information
?
-
-
the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
-
-
?
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1,10-phenanthroline
-
strong inhibition
4-chloromercuribenzoate
-
37% inhibition at 1 mM
Ag+
-
1 mM: complete inhibition
bathophenanthroline
-
complete inhibition, activity fully restored by addition of Fe3+ at a ratio of 4 iron atoms to 1 mol inactive protein, the apoenzyme
Cd2+
-
18% inhibition at 1 mM
ethanol
-
50% inhibition at 30% v/v
F-
-
1 mM: complete inhibition
Fe2+
-
1 mM: 67% inhibition, 10 mM: complete inhibition
iodoacetic acid
-
0.1 mM: 40% inhibition
N-Benzoylphosphoric triamide
-
-
O,O-Dimethyl-O-(2,2-dichlorovinyl) phosphate
-
-
O,O-Dimethyl-O-(3-methyl-4-nitrophenyl) phosphate
-
-
p-chloromercuribenzoate
-
0.1 mM: 52% inhibition
phenylmethylsulfonyl fluoride
phenylphosphorodiamide
-
-
phenylthiophosphorodiamide
-
-
PMSF
-
84% inhibition at 1 mM
Sodium laurylsulfate
-
35 mM: complete inhibition
Co2+
-
1 mM: 41% inhibition, 20 mM: complete inhibition
Co2+
-
11% inhibition at 1 mM
Cu2+
-
1 mM: 37% inhibition, 20 mM: 69% inhibition
Cu2+
-
61% inhibition at 1 mM
EDTA
-
no inhibition
EDTA
-
strong inhibition, 0.00074 mM: 50% inhibition. Complete inhibition fully recovered by addition of Zn2+, but no activity recovered by addition of Mg2+
Hg2+
-
1 mM: complete inhibition
Hg2+
-
98% inhibition at 1 mM
iodoacetamide
-
no inhibition at 0.1 mM
iodoacetamide
-
0.1 mM: 48% inhibition
Ni2+
-
1 mM: 14% inhibition, 20 mM: 58% inhibition
Ni2+
-
32% inhibition at 1 mM
phenylmethylsulfonyl fluoride
-
PMSF
phenylmethylsulfonyl fluoride
-
0.1 mM: 61% inhibition; PMSF
Zn2+
-
1 mM: 29% inhibition, 25 mM: complete inhibition
Zn2+
-
21% inhibition at 1 mM
additional information
-
no inhibition by 1 mM EDTA or 1 mM EGTA
-
additional information
-
no inhibition by 1 mM EDTA and 2-mercaptoethanol
-
additional information
-
no inhibition by 1 mM EDTA and 2-mercaptoethanol; no inhibition by diethyldicarbonate, N-ethylmaleimide or iodoacetamide at 0.1 mM
-
additional information
-
no inhibition by EDTA
-
additional information
-
no or poor inhibition by Mn2+, EDTA, 8-hydroxyquinoline, DTT, and iodoacetamide
-
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additional information
-
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively
additional information
-
development of an amperometric biosensor for ethyl carbamate (urethane) with urethanase and glutamate dehydrogenase (GLDH). Urethanase decomposes ethyl carbamate to produce ammonia, which is converted to L-glutamate under the catalysis of GLDH in the presence of 2-oxoglutarate and NADH. The two enzymes are entrapped into chitosan/gelatine/gamma-glycidoxy propyl trimethoxy silane sol-gel and immobilized on the surface of pyrolytic graphite electrode (PGE). The modified electrode is characterized by cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). Under the optimized conditions, the amperometric EC biosensor exhibits a linear detection range from 0.0005 to 0.040 mM with a low detection limit of 5.30 nM. The biosensor is successfully used to detect urethane in mimic Chinese rice wine samples, and satisfactory recovery and relative standard deviation are achieved
additional information
-
development of an amperometric biosensor for ethyl carbamate (urethane) with urethanase and glutamate dehydrogenase (GLDH). Urethanase decomposes ethyl carbamate to produce ammonia, which is converted to L-glutamate under the catalysis of GLDH in the presence of 2-oxoglutarate and NADH. The two enzymes are entrapped into chitosan/gelatine/gamma-glycidoxy propyl trimethoxy silane sol-gel and immobilized on the surface of pyrolytic graphite electrode (PGE). The modified electrode is characterized by cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). Under the optimized conditions, the amperometric EC biosensor exhibits a linear detection range from 0.0005 to 0.040 mM with a low detection limit of 5.30 nM. The biosensor is successfully used to detect urethane in mimic Chinese rice wine samples, and satisfactory recovery and relative standard deviation are achieved
-
additional information
-
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively
-
additional information
-
development of an amperometric biosensor for ethyl carbamate (urethane) with urethanase and glutamate dehydrogenase (GLDH). Urethanase decomposes ethyl carbamate to produce ammonia, which is converted to L-glutamate under the catalysis of GLDH in the presence of 2-oxoglutarate and NADH. The two enzymes are entrapped into chitosan/gelatine/gamma-glycidoxy propyl trimethoxy silane sol-gel and immobilized on the surface of pyrolytic graphite electrode (PGE). The modified electrode is characterized by cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). Under the optimized conditions, the amperometric EC biosensor exhibits a linear detection range from 0.0005 to 0.040 mM with a low detection limit of 5.30 nM. The biosensor is successfully used to detect urethane in mimic Chinese rice wine samples, and satisfactory recovery and relative standard deviation are achieved
-
additional information
-
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively
-
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analysis
-
the enzyme is used in spectrophotometric determination of ethyl carbamate through bi-enzymatic cascade reactions, method, overview. Detection of ethyl carbamate (urethane) in Chinese rice wine. Urethane is known as a genotoxic carcinogen1 that widely exists in fermented foods and alcoholic beverages, such as bread, yogurt, cheese, brandy, Chinese rice wine, sake, and wine, due to the natural biochemical processes in the fermentation process
analysis
-
the enzyme is used in spectrophotometric determination of ethyl carbamate through bi-enzymatic cascade reactions, method, overview. Detection of ethyl carbamate (urethane) in Chinese rice wine. Urethane is known as a genotoxic carcinogen1 that widely exists in fermented foods and alcoholic beverages, such as bread, yogurt, cheese, brandy, Chinese rice wine, sake, and wine, due to the natural biochemical processes in the fermentation process
-
food industry
-
urethanase is useful to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine, strain CGMCC 5081 culture condition optimization for enzyme production in immobilized cells
food industry
-
with good ethanol tolerance, the crude urethanase is able to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine without the change of flavor substance in wine
food industry
-
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) have great potential in the elimination of urethane (ethyl carbamate) from Chinese rice wine. Process flow diagram of PRU-CLEAs applied in membrane reactor, overview
food industry
-
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) have great potential in the elimination of urethane (ethyl carbamate) from Chinese rice wine. Process flow diagram of PRU-CLEAs applied in membrane reactor, overview
-
food industry
-
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) have great potential in the elimination of urethane (ethyl carbamate) from Chinese rice wine. Process flow diagram of PRU-CLEAs applied in membrane reactor, overview
-
food industry
-
urethanase is useful to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine, strain CGMCC 5081 culture condition optimization for enzyme production in immobilized cells
-
food industry
-
with good ethanol tolerance, the crude urethanase is able to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine without the change of flavor substance in wine
-
nutrition
-
practically ineffective for the elimination of urethane from alcoholic beverages, because the enzyme is inactive in high concentrations of alcohol, ethanol, and at acidic pH
nutrition
-
enzyme may be practically applicable in removal of urethane from alcoholic beverages, because very high ethanol resistance, high activity at acidic condition, pH 5.0 and very low Km value for urethane
nutrition
-
great advantage for industrial removal of urethane, potentially carcinogenic, mutagenic and teratogenic to human, from alcoholic beverages
nutrition
-
great advantage for industrial removal of urethane, potentially carcinogenic, mutagenic and teratogenic to human, from alcoholic beverages
nutrition
-
great advantage for industrial removal of urethane, potentially carcinogenic, mutagenic and teratogenic to human, from alcoholic beverages
nutrition
-
strain IFO 12107, enzyme may be a practical means of removing urethane from alcoholic beverages, because its higher activity under acidic conditions, pH 4.5, its high ethanol resistance and its low Km value for urethane
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