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Literature summary extracted from

  • Ray, R.R.; Jana, S.C.; Nanda, G.
    Biochemical approaches of increasing thermostability of beta-amylase from Bacillus megaterium B6 (1994), FEBS Lett., 356, 30-32.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.2 immobilization of beta-amylase through gel-entrapment and covalent crosslinking brings about a remarkable increase in thermotolerance with about a 14-fold increase in catalytic half-life Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Priestia megaterium
-
-
-
3.2.1.2 Priestia megaterium B6
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 starch + H2O
-
Priestia megaterium maltose + ?
-
?
3.2.1.2 starch + H2O
-
Priestia megaterium B6 maltose + ?
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 additional information
-
increased thermoresistance of beta-amylase is achieved through stabilization of thiol groups present at the active site by manipulating the enzyme’s environment by the addition of Mn2+ and 2-mercaptoethanol, and through immobilization. Both of which would increase the enzyme’s practical importance and industrial utility Priestia megaterium
3.2.1.2 60
-
the thermoinactivated enzyme (exposed to 60°C for 10 min) could be partially reactivated by the addition of 1 mM 2-mercaptoethanol (7.3% increase) and 4 mM Mn2+ (14% increase) Priestia megaterium