Literature summary for 1.1.3.4 extracted from

Halalipour, A.; Duff, M.R.; Howell, E.E.; Reyes-De-Corcuera, J.I.
Catalytic activity and stabilization of phenyl-modified glucose oxidase at high hydrostatic pressure (2020), Enzyme Microb. Technol., 137, 109538 .

General Stability

General Stability	Organism
high hydrostatic pressure stabilizes the aniline-, and benzoate-modified glucose oxidase at 69.1-80°C compared to atmospheric pressure. At 240 MPa and 80.0°C, the first order rate constant of inactivation (k(inact)) of aniline-modified enzyme is 0.02/min, or 3.7 times smaller than for the native enzyme, while the k(inact) for benzoate-modified enzyme is 0.26/min, or 2.8times smaller than for the native enzyme at the same temperature. At 240 MPa and 80.0°C, the k(inact) of the aniline-modified enzyme is 69times smaller than the k(inact) of native enzyme (15.3/min) at 0.1 MPa and 80.0°C. The combination of high hydrostatic pressure and hydrophobic modification makes more thermostable	Aspergillus niger

Organism

high hydrostatic pressure stabilizes the aniline-, and benzoate-modified glucose oxidase at 69.1-80°C compared to atmospheric pressure. At 240 MPa and 80.0°C, the first order rate constant of inactivation (k(inact)) of aniline-modified enzyme is 0.02/min, or 3.7 times smaller than for the native enzyme, while the k(inact) for benzoate-modified enzyme is 0.26/min, or 2.8times smaller than for the native enzyme at the same temperature. At 240 MPa and 80.0°C, the k(inact) of the aniline-modified enzyme is 69times smaller than the k(inact) of native enzyme (15.3/min) at 0.1 MPa and 80.0°C. The combination of high hydrostatic pressure and hydrophobic modification makes more thermostable

Aspergillus niger

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	P13006	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-D-glucose + O2	-	Aspergillus niger	D-glucono-1,5-lactone + H2O2	-	?

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
25	69	at each temperature in the study (25-69.1°C), the catalytic activity of the native, aniline-, or benzoate-modified enzyme increases with high hydrostatic pressure, and reaches a maximum at around 180 MPa. At 180 MPa and 69.1°C, aniline-modified enzyme produces the fastest catalytic rate, followed by benzoate-modified enzyme, and then native enzyme	Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
80	-	at 240 MPa and 80.0°C, the first order rate constant of inactivation (k(inact)) of aniline-modified enzyme is 0.02/min, or 3.7 times smaller than for the native enzyme, while the k(inact) for benzoate-modified enzyme is 0.26/min, or 2.8times smaller than for the native enzyme at the same temperature. At 240 MPa and 80.0°C, the k(inact) of the aniline-modified enzyme is 69times smaller than the k(inact) of native enzyme (15.3/min) at 0.1 MPa and 80.0°C	Aspergillus niger