Claim · model-written summary
With veratryl alcohol substrate, Km was 20 μM.
- Taxon
- citrus sinensis
Citrus sinensist0 - Treatment
- veratryl alcohole0
- Outcome
- Kme0
- Value
- 20 μMe0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingDirectionQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Km and Kcat value using veratryl alcohol and manganese sulphate as a substrate is 20 μM, 7.87sec and 12.5 μM, 13.84sec-1.”
t0“citrus sinensis”
Title
Nivedita Rai; Meera Yadav; Hardeo Singh Yadav Analytical Chemistry Letters 2020. doi:10.1080/22297928.2020.1833751
Other claims from this paper (14)
- Observation Citrus leaf extract had manganese peroxidase activity of 2.2 IU/ml.
- Observation Citrus leaf extract had lignin peroxidase activity of 0.44 IU/ml.
- Observation Peroxidase recovery yield was 11 %.
- Observation Peroxidase specific activity was 1.0 IU/mg.
- Observation Peroxidase molecular weight was 24.60KDa.
- Observation With veratryl alcohol substrate, Kcat was 7.87sec.
- Observation With manganese sulphate substrate, Km was 12.5 μM.
- Observation With manganese sulphate substrate, Kcat was 13.84sec-1.
- Observation Lignin peroxidase activity had pH optimum 2.4 ± 0.1.
- Observation Manganese peroxidase activity had pH optimum 4.5 ± 0.1.
- Observation LiP temperature optimum was 18°C.
- Observation MnP temperature optimum was 25°C.
- Intervention effect Sodium azide effectively inhibited enzyme activity.
- Intervention effect EDTA effectively inhibited enzyme activity.