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Literature summary for 3.1.3.2 extracted from

  • Chang, M.Y.; Juang, R.S.
    Stability and catalytic kinetics of acid phosphatase immobilized on composite beads of chitosan and activated clay (2004), Process Biochem., 39, 1087-1091.
No PubMed abstract available

Application

Application Comment Organism
biotechnology improved stability and catalytic kinetics of acid phosphatase immobilized on composite beads of chitosan and activated clay as a model system for enzyme immobilization optimization Sepia sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Sepia sp.

Organism

Organism UniProt Comment Textmining
Sepia sp.
-
cuttlebone
-

Source Tissue

Source Tissue Comment Organism Textmining
cartilage
-
Sepia sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
the enzyme retains 90% of its activity immobilized on composite beads of chitosan and activated clay Sepia sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Sepia sp. 4-nitrophenol + phosphate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45 57
-
Sepia sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
27 87 activity range, sharp decrease of activity below 47°C and above 67°C Sepia sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
thermal stability/deactivation of the immobilized enzyme, overview Sepia sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3
-
-
Sepia sp.

pH Range

pH Minimum pH Maximum Comment Organism
3.5 6.5
-
Sepia sp.