Keratinase (gene kerT1) from Thermoactinomyces sp. YT06

Enzyme Description

Extremophile
Yes "thermophilic" organism
EC Number

Sequence

Length: 278 amino acids
TPNDPRYSEQYAPQLVGAEEAWDVTQGSSNVTVAIVDTGVDYTHPDLQGKVVKGKDFVDNDDDPMDENMHGTHCAGIAAALTNNGVGIAGMAPKVKILAERVLDANGSGTLDSVAQGITHAADQGADVISLSLGSPQGASTLEDAVNYAASKGAVVVAAAGNESTSAPSYPAYYEKAIAVAATDSNDRIASFSNYGSWVDVAAPGVNILSTVPGGGYQTASGTSMATPLVAGQAALLASQGKSASEIRQAIEGTADKISGTGQYWAHGRVNAAKSVSQ
Lin Wang et al. (2019) β€” Cloning and expression of a thermostable keratinase gene from Thermoactinomyces sp. YT06 in Escherichia coli and characterization of purified recombinant enzymes
World Journal of Microbiology and Biotechnology  Β· doi:10.1007/s11274-019-2710-1 β†—  Β· Activity - Classical
8 measurements
Database ID
Sequence Annotation
Explicit - Provided (111 first residues from UniProt sequence absent from the mature protein)
Protein Source
Recombinant, host bacterium Escherichia coli BL21 (DE3)

Experimental Data (8 measurements)

8 measurements
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu phenol reagant and free tyrosines reaction product absorbance measurement, 660 nm) 1-Propanol 10% 100.0 16.3 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu pheno reagant reacting with tyrosines, 660 nm) Acetone 10% 100.0 82.2 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu pheno reagant reacting with tyrosines, 660 nm) Dimethyl Sulfoxide (DMSO) 10% 100.0 91.5 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu pheno reagant reacting with tyrosines, 660 nm) Xylene 10% 100.0 96.5 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu pheno reagant reacting with tyrosines, 660 nm) 1-Butanol 10% 100.0 6.0 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu pheno reagant reacting with tyrosines, 660 nm) Toluene 10% 100.0 97.4 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu pheno reagant reacting with tyrosines, 660 nm) 1-Octanol 10% 100.0 89.5 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference
Activity - Classical Activity measured by absorbance spectrophotometry (colorimetric assay, Folin-Ciocalteu pheno reagant reacting with tyrosines, 660 nm) Ethanol 10% 100.0 57.8 % 33.3 mM glycine-NaOH buffer 9 65Β°C 0.033 % (w/v) Soluble keratine free amino acids , Peptides β€” β€” Correct contol (in %) | Assay conditions taken from reference

Visualization : Activity β€” Classical

One bar per measurement. Colour = solvent, shade = solvent volume.

Structure

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