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Literature summary extracted from

  • Sagu, S.; Nso, E.; Homann, T.; Kapseu, C.; Rawel, H.
    Isolation and purification of beta-amylase from stems of Cadaba farinosa and determination of its characteristics (2016), Curr. Top. Pept. Protein Res., 17, 21-35 .
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.2 acetic acid 75% inhibition at 10 mM, 16.3% inhibition at 1 mM Cadaba farinosa
3.2.1.2 Citric acid complete inhibition at 5-10 mM, 84.7% inhibition at 1 mM Cadaba farinosa
3.2.1.2 CuSO4 over 94% inhibition at 1-10 mM Cadaba farinosa
3.2.1.2 FeCl3 complete inhibition at 1-10 mM Cadaba farinosa
3.2.1.2 Lactic acid complete inhibition at 10 mM, 58.3% inhibition at 1 mM Cadaba farinosa
3.2.1.2 additional information no or poor effect by boric acid and urea at 1-10 mM Cadaba farinosa
3.2.1.2 salicylic acid complete inhibition at 10 mM, 61.4% inhibition at 1 mM Cadaba farinosa
3.2.1.2 Tannic acid complete inhibition at 10 mM, 81.8% inhibition at 1 mM Cadaba farinosa
3.2.1.2 ZnSO4 15% inhibition at 10 mM, no inhibition at 1 mM Cadaba farinosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.2 additional information
-
 additional information Michaelis-Menten kinetics and Lineweaver-Burk plots, Km and Vmax values at 50°C are estimated to be 2.81 mg/ml and 10.62 U/min, respectively Cadaba farinosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.2 Ag+ activates 12% at 10 mM Cadaba farinosa
3.2.1.2 Ca2+ activates 11% at 10 mM Cadaba farinosa
3.2.1.2 K+ activates 10% at 10 mM Cadaba farinosa
3.2.1.2 Na+ activates 11% at 10 mM Cadaba farinosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.2 starch + H2O Cadaba farinosa beta-amylase is an exo-amylase acting on starch with the successive removal of maltose molecules from the non-reducing ends of the glucose polymers with inversion of the anomeric configuration ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Cadaba farinosa
-
 collected from Yagoua, a town of Mayo-Danay department, located in the Far North region, Cameroon
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2 native enzyme from powdered stems by three-phase partitioning (TPP), method evaluation and optimization, and model validation, overview Cadaba farinosa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.2 stem
-
 Cadaba farinosa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 starch + H2O beta-amylase is an exo-amylase acting on starch with the successive removal of maltose molecules from the non-reducing ends of the glucose polymers with inversion of the anomeric configuration Cadaba farinosa ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.2 ? x * 63000, SDS-PAGE Cadaba farinosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 50
-
 assay at Cadaba farinosa

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.2 50 70 high activity range Cadaba farinosa

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 20 60 purified native enzyme, 1 h, pH 6.0, stable Cadaba farinosa
3.2.1.2 80
-
 purified native enzyme, 1 h, pH 6.0, 80% activity remaining Cadaba farinosa
3.2.1.2 90
-
 purified native enzyme, 1 h, pH 6.0, 5% activity remaining Cadaba farinosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 6.5
-
-
 Cadaba farinosa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.2 5 7 high activity range Cadaba farinosa

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.2 5 7 purified native enzyme, 4°C, 4 h, over 65% activity remaining, rapid and almost complete loss of activity above Cadaba farinosa