Any feedback?
Literature summary for 3.2.1.40 extracted from
- Expression and biochemical characterization of recombinant alpha-L-rhamnosidase r-Rha1 from Aspergillus niger JMU-TS528 (2016), Int. J. Biol. Macromol., 85, 391-399 .
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications | Aspergillus niger |
| food industry | the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications | Aspergillus niger |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression in Pichia pastoris GS115s | Aspergillus niger |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | 100 mM, complete inactivation | Aspergillus niger |  |
| Fe3+ | 10 mM, 46% inhibition. 100 mM, 91% inhibition | Aspergillus niger | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 10 mM, 1.1fold activation. 100 mM, 1.4fold activation | Aspergillus niger | |
| Co2+ | 10 mM, 1.1fold activation. 100 mM, 1.6fold activation | Aspergillus niger | |
| Cu2+ | 10 mM, 1.2fold activation. 100 mM, 1.3fold activation | Aspergillus niger | |
| Fe2+ | 10 mM, 1.1fold activation | Aspergillus niger | |
| Mg2+ | 10 mM or 100 mM, 1.1fold activation | Aspergillus niger | |
| Mn2+ | 100 mM, 1.5fold activation | Aspergillus niger | |
| Ni2+ | 100 mM, 1.5fold activation | Aspergillus niger | |
| Zn2+ | 10 mM, 1.1fold activation. 100 mM, 1.5fold activation | Aspergillus niger | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | R9W5L0 | - |
- |
| Aspergillus niger JMU-TS528 | R9W5L0 | - |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 711.9 | - |
activity of the recombinant overexpressed enzyme, pH and temperature not specified in the publication | Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl alpha-L-rhamnopyranoside + H2O | 70.1% of the activity compared to naringin | Aspergillus niger | 4-nitrophenol + alpha-L-rhamnopyranose | - |
? | |
| 4-nitrophenyl alpha-L-rhamnopyranoside + H2O | 70.1% of the activity compared to naringin | Aspergillus niger JMU-TS528 | 4-nitrophenol + alpha-L-rhamnopyranose | - |
? | |
| hesperidin + H2O | 144.9% of the activity compared to naringin | Aspergillus niger | hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose | - |
? | |
| hesperidin + H2O | 144.9% of the activity compared to naringin | Aspergillus niger JMU-TS528 | hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose | - |
? | |
| additional information | the enzyme posseses broad substrate specificities by hydrolyzing alpha-1,2, alpha-1,3 alpha-1,4, and alpha-1,6 linkages to beta-D-glucosides | Aspergillus niger | ? | - |
? | |
| additional information | the enzyme posseses broad substrate specificities by hydrolyzing alpha-1,2, alpha-1,3 alpha-1,4, and alpha-1,6 linkages to beta-D-glucosides | Aspergillus niger JMU-TS528 | ? | - |
? | |
| myricetrin + H2O | 22.5% of the activity compared to naringin | Aspergillus niger | 3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose | - |
? | |
| naringin + H2O | - |
Aspergillus niger | beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose | - |
? | |
| naringin + H2O | - |
Aspergillus niger JMU-TS528 | beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose | - |
? | |
| rutin + H2O | 136.7% of the activity compared to naringin | Aspergillus niger | isoquercitrin + alpha-L-rhamnose | - |
? | |
| rutin + H2O | 136.7% of the activity compared to naringin | Aspergillus niger JMU-TS528 | isoquercitrin + alpha-L-rhamnose | - |
? | |
| saikosaponin C + H2O | 9.19% of the activity compared to naringin | Aspergillus niger | (3beta,16beta)-16-hydroxy-13,28-epoxyolean-11-en-3-yl) 6-O-beta-D-glucopyranosyl-beta-D-glucopyranoside + alpha-L-rhamnose | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Aspergillus niger |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 70 | 30°C: about 65% of maximal activity, 70°C: about 55% of maximal activity | Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
half-life time: 32.66 h | Aspergillus niger |
| 55 | - |
half-life time: 15.44 h | Aspergillus niger |
| 60 | - |
half-life time: 2.59 h | Aspergillus niger |
| 65 | - |
half-life time: 18.7 min | Aspergillus niger |
| 70 | - |
half-life time: 4.6 min | Aspergillus niger |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
- |
Aspergillus niger |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 11 | 24 h, 4°C, more than 45% of its enzymatic activity is retained | Aspergillus niger |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
