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Literature summary for 3.2.1.3 extracted from

  • Takahashi, T.; Tsuchida, Y.; Irie, M.
    Purification and some properties of three forms of glucoamylase from a Rhizopus species (1978), J. Biochem., 84, 1183-1194.
    View publication on PubMed
Search for more literature for 3.2.1.3

Inhibitors

Inhibitors Comment Organism Structure
Hg2+ 1 mM, 64-70% inhibition Rhizopus sp.
Mn2+ 1 mM, 20-29% inhibition Rhizopus sp.
Pb2+ 1 mM, 20-29% loss of activity Rhizopus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58600
-
 glucoamylase 2, ultracentrifugal equilibrium sedimentation Rhizopus sp.
61400
-
 glucoamylase 3, ultracentrifugal equilibrium sedimentation Rhizopus sp.
74000
-
 glucoamylase 1, ultracentrifugal equilibrium sedimentation Rhizopus sp.

Organism

Organism UniProt Comment Textmining
Rhizopus sp.
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Rhizopus sp.

Purification (Commentary)

Purification (Comment) Organism
three enzyme forms: glucoamylase 1, 2 and 3 Rhizopus sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Rhizopus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 pH 6.0, 5 min, stable Rhizopus sp.
60
-
 pH 6.0, 5 min, complete inactivation Rhizopus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5 5
-
 Rhizopus sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 8 37°C, 1 h, stable Rhizopus sp.