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Literature summary for 3.2.1.22 extracted from

  • Cao, Y.; Wang, Y.; Luo, H.; Shi, P.; Meng, K.; Zhou, Z.; Zhang, Z.; Yao, B.
    Molecular cloning and expression of a novel protease-resistant GH-36 alpha-galactosidase from Rhizopus sp. F78 ACCC 30795 (2009), J. Microbiol. Biotechnol., 19, 1295-1300.
    View publication on PubMed
Search for more literature for 3.2.1.22

Activating Compound

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(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Rhizopus sp. ACCC 30795

General Stability

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

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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
82000
-
 3 * 82000, SDS-PAGE Rhizopus sp. ACCC 30795
210000
-
 gel filtration Rhizopus sp. ACCC 30795

Organism

Organism UniProt Comment Textmining
Rhizopus sp. ACCC 30795 C7SEV1
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Rhizopus sp. ACCC 30795

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Subunits Comment Organism
homotrimer 3 * 82000, SDS-PAGE Rhizopus sp. ACCC 30795

Synonyms

Synonyms Comment Organism
Aga-F78
-
 Rhizopus sp. ACCC 30795

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Rhizopus sp. ACCC 30795

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.8
-
-
 Rhizopus sp. ACCC 30795

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 10 highly pH stable over the pH range 5.0-10.0 Rhizopus sp. ACCC 30795

pI Value

Organism Comment pI Value Maximum pI Value
Rhizopus sp. ACCC 30795 calculated from amino acid sequence
-
 5.4