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Literature summary for 3.2.1.2 extracted from

  • Murao, S.; Ohyama, K.; Arai, M.
    beta-Amylases from Bacillus polymyxa No. 72 (1979), Agric. Biol. Chem., 43, 719-726.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
PCMB cysteine reactivates Paenibacillus polymyxa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
beta-amylase I and II, gel filtration Paenibacillus polymyxa

Organism

Organism UniProt Comment Textmining
Paenibacillus polymyxa
-
No. 72
-
Paenibacillus polymyxa No. 72
-
No. 72
-

Purification (Commentary)

Purification (Comment) Organism
beta-amylase I and II Paenibacillus polymyxa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Paenibacillus polymyxa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O
-
Paenibacillus polymyxa maltose + ? beta-maltose ?
starch + H2O
-
Paenibacillus polymyxa No. 72 maltose + ? beta-maltose ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Paenibacillus polymyxa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
10 min, stable below Paenibacillus polymyxa
60
-
10 min, about 70% loss of activity Paenibacillus polymyxa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Paenibacillus polymyxa

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 9 15 h, 37°C, stable Paenibacillus polymyxa