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Literature summary for 3.2.1.2 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
Search for more literature for 3.2.1.2

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

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

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
stem
-
 Cadaba farinosa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Cadaba farinosa

pH Range

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

pH Stability

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