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Literature summary extracted from

  • Feng, B.; Hu, W.; Ma, B.P.; Wang, Y.Z.; Huang, H.Z.; Wang, S.Q.; Qian, X.H.
    Purification, characterization, and substrate specificity of a glucoamylase with steroidal saponin-rhamnosidase activity from Curvularia lunata (2007), Appl. Microbiol. Biotechnol., 76, 1329-1338.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.3 synthesis the enzyme is industrially an important biocatalyst that decomposes starch into glucose by tearing-off alpha-1,4-linked glucose residue from the non-reduced end of the polysaccharide chain Curvularia lunata

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.3 66000
-
 x * 66000, SDS-PAGE Curvularia lunata

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Curvularia lunata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.3 native enzyme 5.0fold by ammonium sulfate fractionation, gel filtration, and cation and anion exchange chromatography to homogeneity Curvularia lunata

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.3 2.54
-
 culture supernatant, substrate starch Curvularia lunata
3.2.1.3 19.73
-
 purified enzyme, substrate starch Curvularia lunata

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 additional information the glucoamylase also shows steroidal saponin-rhamnosidase activity, EC 3.2.1.40, being able to hydrolyze the terminal rhamnosyl of steroidal saponins and the sugar chain at the C-3 position of spirostanosides, the enzyme also hydrolyzed the terminal rhamnosyl residues of the sugar chain at the C-3 position while retaining the glucosyl residues at the C-26 position of furostanosides, substrate specificity, overview Curvularia lunata ?
-
 ?
3.2.1.3 starch + H2O soluble starch Curvularia lunata ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.3 ? x * 66000, SDS-PAGE Curvularia lunata
3.2.1.3 More enzyme amino acid sequence analysis by MALDI-TOF mass spectrometry Curvularia lunata

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 1,4-alpha-D-glucan glucohydrolase
-
 Curvularia lunata
3.2.1.3 glucoamylase
-
 Curvularia lunata

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 50
-
-
 Curvularia lunata

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.3 20 70
-
 Curvularia lunata

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 20
-
 purified enzyme, 30-40% remaining activity Curvularia lunata
3.2.1.3 30
-
 purified enzyme, stable Curvularia lunata
3.2.1.3 30 40 purified enzyme, 80% of maximal activity within this range Curvularia lunata
3.2.1.3 50
-
 purified enzyme, 70% remaining activity Curvularia lunata
3.2.1.3 70
-
 purified enzyme, 30-40% remaining activity Curvularia lunata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 4
-
-
 Curvularia lunata

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.3 3 8
-
 Curvularia lunata

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.3 3
-
 purified enzyme, 60% remaining activity Curvularia lunata
3.2.1.3 4 7 purified enzyme, 90% of maximal activity within this range Curvularia lunata