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Literature summary for 3.1.1.20 extracted from

  • Wu, C.; Xu, C.; Ni, H.; Yang, Q.; Cai, H.; Xiao, A.
    Preparation and characterization of tannase immobilized onto carboxyl-functionalized superparamagnetic ferroferric oxide nanoparticles (2016), Biores. Technol., 205, 67-74 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information preparation of tannase immobilized onto carboxyl-functionalized superparamagnetic ferroferric oxide nanoparticles (CMNPs) by glutaraldehyde (best at 3.5% v/v), method evaluation and optimization, overview. The activity of the immobilized tannase reaches 85.35 U/g carrier after 24 h of immobilization. Successful binding between CMNPs and tannase is confirmed by Fourier transform infrared spectroscopy and thermogravimetric analysis. Vibrating sample magnetometry and X-ray diffraction show that the CMNPs and immobilized tannase exhibit distinct magnetic responses and superparamagnetic properties. The thermal, pH, and storage stabilities of the immobilized tannase are superior to those of free tannase. Immobilized tannase is more stable than free tannase at pH -8 with over 80% residual enzyme activity. After six cycles of catalytic hydrolysis of propyl gallate, the immobilized tannase maintains over 60% of its initial activity. The Michaelis constant (Km) of the immobilized enzyme indicates its higher affinity for substrate binding than the free enzyme Aspergillus tubingensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Aspergillus tubingensis
0.29
-
propyl gallate immobilized enzyme, pH 5.0, 30°C Aspergillus tubingensis
0.45
-
propyl gallate free enzyme, pH 5.0, 30°C Aspergillus tubingensis

Organism

Organism UniProt Comment Textmining
Aspergillus tubingensis
-
-
-
Aspergillus tubingensis CICC 2651
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information for activity detection, the produced gallic acid is combined with alcoholic rhodanine to form a chromogen, that is spectrometrically measured Aspergillus tubingensis ?
-
?
additional information for activity detection, the produced gallic acid is combined with alcoholic rhodanine to form a chromogen, that is spectrometrically measured Aspergillus tubingensis CICC 2651 ?
-
?
propyl gallate + H2O
-
Aspergillus tubingensis propanol + gallic acid
-
?
propyl gallate + H2O
-
Aspergillus tubingensis CICC 2651 propanol + gallic acid
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
free and immobilized enzyme Aspergillus tubingensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 70 activity range Aspergillus tubingensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4
-
free enzyme Aspergillus tubingensis
7
-
immobilized enzyme Aspergillus tubingensis

pH Range

pH Minimum pH Maximum Comment Organism
4 8 activity range Aspergillus tubingensis