Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | the activity of recombinant Aga-F78 is significantly enhanced in the presence of EDTA | Rhizopus sp. ACCC 30795 |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21(DE3) cells | Rhizopus sp. ACCC 30795 |
General Stability | Organism |
---|---|
the enzyme is protease-resistant, when combined with trypsin, the enzyme retained over 90% degradability to soybean meal | Rhizopus sp. ACCC 30795 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ag+ | strong inhibitor | Rhizopus sp. ACCC 30795 | |
Hg2+ | strong inhibitor | Rhizopus sp. ACCC 30795 | |
Mn2+ | strong inhibitor | Rhizopus sp. ACCC 30795 | |
SDS | strong inhibitor | Rhizopus sp. ACCC 30795 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cr3+ | the activity of recombinant Aga-F78 is significantly enhanced in the presence of Cr3+ | Rhizopus sp. ACCC 30795 | |
Fe3+ | the activity of recombinant Aga-F78 is significantly enhanced in the presence of Fe3+ | Rhizopus sp. ACCC 30795 | |
additional information | the addition of other metal ions or chemicals has little or no effect on the activity | Rhizopus sp. ACCC 30795 | |
Pb2+ | the activity of recombinant Aga-F78 is significantly enhanced in the presence of Pb2+ | Rhizopus sp. ACCC 30795 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
82000 | - |
3 * 82000, SDS-PAGE | Rhizopus sp. ACCC 30795 |
210000 | - |
gel filtration | Rhizopus sp. ACCC 30795 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhizopus sp. ACCC 30795 | C7SEV1 | - |
- |
Purification (Comment) | Organism |
---|---|
Ni-NTA column chromatography | Rhizopus sp. ACCC 30795 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
56.61 | - |
after 2461.3fold purification, using 4-nitrophenyl alpha-D-galactoside as substrate, at 37°C | Rhizopus sp. ACCC 30795 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl alpha-D-galactoside + H2O | - |
Rhizopus sp. ACCC 30795 | 4-nitrophenol + alpha-D-galactose | - |
? | |
melibiose + H2O | - |
Rhizopus sp. ACCC 30795 | D-galactose + D-glucose | - |
? | |
raffinose + H2O | - |
Rhizopus sp. ACCC 30795 | sucrose + alpha-D-galactose | - |
? | |
stachyose + 2 H2O | - |
Rhizopus sp. ACCC 30795 | 2 alpha-D-galactose + sucrose | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotrimer | 3 * 82000, SDS-PAGE | Rhizopus sp. ACCC 30795 |
Synonyms | Comment | Organism |
---|---|---|
Aga-F78 | - |
Rhizopus sp. ACCC 30795 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
- |
Rhizopus sp. ACCC 30795 |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 60 | the recombinant enzyme loses about 60% of the initial activity after incubation at 50°C for 30 min and is completely inactivated at 60°C for 5 min | Rhizopus sp. ACCC 30795 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.8 | - |
- |
Rhizopus sp. ACCC 30795 |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5 | 10 | highly pH stable over the pH range 5.0-10.0 | Rhizopus sp. ACCC 30795 |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Rhizopus sp. ACCC 30795 | calculated from amino acid sequence | - |
5.4 |