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Literature summary for 3.2.1.2 extracted from

  • Germain, P.; Crichton, R.R.
    Characterization of a chemically modified beta-amylase immobilized on porous silica (1988), J. Chem. Technol. Biotechnol., 41, 297-315.
No PubMed abstract available

General Stability

General Stability Organism
immobilization of both native and modified enzymes on a amino silica results in thermostabilization of the enzyme Ipomoea batatas

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Ipomoea batatas

Organism

Organism UniProt Comment Textmining
Ipomoea batatas
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O soluble Ipomoea batatas maltose + ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
native immobilized beta-amylase Ipomoea batatas
75
-
chemically modified and subsequently immobilized beta-amylase Ipomoea batatas

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
immobilization of both native and modified enzymes on a amino silica results in thermostabilization of the enzyme Ipomoea batatas