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Literature summary extracted from

  • Shi, X.; Zhao, L.; Pei, J.; Ge, L.; Wan, P.; Wang, Z.; Xiao, W.
    Highly enhancing the characteristics of immobilized thermostable beta-glucosidase by Zn2+ (2018), Process Biochem., 66, 89-96 .
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.21 Zn2+ presence of 2 mM Zn2+ increases the relative activity of the immobilized enzyme to 192% and 199% with cellobiose and 4-nitrophenyl-beta-D-glucopyranoside as substrates Thermotoga petrophila

Application

EC Number Application Comment Organism
3.2.1.21 industry the enzyme is widely used in cellulose hydrolysis and the biological conversion and transformation of flavonoids and saponins. The properties of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde, including thermal stability, pH stability, reusability, and tolerance of glucose, are greatly improved compared with free Tpebgl3. The coordinating metal cation Zn2+ enables the immobilized enzyme to exhibit higher catalytic efficiency. The addition of Zn2+ can greatly advance the reusability, thermostability, and glucose tolerance of immobilized enzyme, which is beneficial for industrial applications Thermotoga petrophila
3.2.1.21 synthesis immobilization of enzyme on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde. The optimal conditions of immobilized enzyme are the same as that of the free enzyme, the highest activity with cellobiose as the substrate approaches 1.7 U/g. Immobilization improves the thermostability, pH stability and glucose tolerance, the residual activity is 68% of the initial activity at the end of 10 repeated cycles. 2 mM Zn2+ increases the relative activity of the immobilized enzyme to 192% and 199% with cellobiose and 4-nitrophenyl-beta-D-glucopyranoside as substrates, respectively and improves the reusability, high-temperature stability, and glucose tolerance Thermotoga petrophila

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.21 expression in Escherichia coli Thermotoga petrophila

General Stability

EC Number General Stability Organism
3.2.1.21 the residual activity of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde is 68% of the initial activity at the end of 10 repeated cycles Thermotoga petrophila
3.2.1.21 Zn2+ greatly improves the reusability, glucose tolerance and high-temperature stability of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde Thermotoga petrophila

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.21 D-glucose when the glucose concentration is 400 mM, the native enzyme is completely inactivated, and the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde with 2mM Zn2+ maintains 63% of its initial activity, which is 19.5% higher than the activity of immobilized enzyme in the absence of Zn2+ Thermotoga petrophila

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.21 2.32
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, without Zn2+ Thermotoga petrophila
3.2.1.21 3.03
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, 2 mM Zn2+ Thermotoga petrophila

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.21 Zn2+ 2 mM Zn2+ increases the relative activity of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde to 192% and 199% with cellobiose and 4-nitrophenyl beta-D-glucopyranoside as substrates, respectively Thermotoga petrophila

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Thermotoga petrophila
-
-
-
3.2.1.21 Thermotoga petrophila A5IL43
-
-
3.2.1.21 Thermotoga petrophila DSM 13995
-
-
-
3.2.1.21 Thermotoga petrophila DSM 13995 A5IL43
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Thermotoga petrophila 4-nitrophenol + D-glucopyranose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Thermotoga petrophila DSM 13995 4-nitrophenol + D-glucopyranose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Thermotoga petrophila nitrophenol + D-glucose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Thermotoga petrophila DSM 13995 nitrophenol + D-glucose
-
 ?
3.2.1.21 cellobiose + H2O
-
 Thermotoga petrophila 2 D-glucose
-
 ?
3.2.1.21 cellobiose + H2O the highest activity with cellobiose as the substrate approaches 1.7 U/g, native enzyme and enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde Thermotoga petrophila 2 D-glucose
-
 ?
3.2.1.21 cellobiose + H2O
-
 Thermotoga petrophila DSM 13995 2 D-glucose
-
 ?
3.2.1.21 cellobiose + H2O the highest activity with cellobiose as the substrate approaches 1.7 U/g, native enzyme and enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde Thermotoga petrophila DSM 13995 2 D-glucose
-
 ?
3.2.1.21 cellulose + H2O
-
 Thermotoga petrophila ?
-
 ?
3.2.1.21 cellulose + H2O
-
 Thermotoga petrophila DSM 13995 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.21 Bgl3
-
 Thermotoga petrophila
3.2.1.21 Tpebgl3
-
 Thermotoga petrophila

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.21 90
-
-
 Thermotoga petrophila
3.2.1.21 90
-
 optimal temperature of native enzyme and of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde Thermotoga petrophila

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.21 60 95 60°C: about 50% of maximal activity, 95°C: about 65% of maximal activity, native enzyme Thermotoga petrophila
3.2.1.21 60 95 60°C: about 50% of maximal activity, 95°C: about 75% of maximal activity, enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde Thermotoga petrophila

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.21 85
-
 7 h, 84% of the residual activity of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde is retained, 63% of the residual activity of the native enzyme is retained. The temperature stability of the immobilized enzyme is better than that of the free enzyme Thermotoga petrophila

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.21 26.89
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, without Zn2+ Thermotoga petrophila
3.2.1.21 51.43
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, 2 mM Zn2+ Thermotoga petrophila

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.21 5
-
-
 Thermotoga petrophila
3.2.1.21 5
-
 optimal pH-value of native enzyme and of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde Thermotoga petrophila

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.21 4 7 pH 4.0: about 65% of maximal activity, pH 7.0: about 45% of maximal activity, enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde Thermotoga petrophila
3.2.1.21 4.5 6 pH 4.5: about 85% of maximal activity, pH 6.0: about 65% of maximal activity, native enzyme Thermotoga petrophila

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.21 3.5
-
 42% of the initial activity for the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde remains, the activity of free enzyme is completely lost Thermotoga petrophila
3.2.1.21 8
-
 the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde retains 79.6% of the initial activity underalkaline conditions (pH 8.0), which is higher by 32% compared with native enzyme Thermotoga petrophila

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.21 11.6
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, without Zn2+ Thermotoga petrophila
3.2.1.21 17
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, 2 mM Zn2+ Thermotoga petrophila