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Literature summary extracted from

  • Siddiqui, K.S.; Poljak, A.; De Francisci, D.; Guerriero, G.; Pilak, O.; Burg, D.; Raftery, M.J.; Parkin, D.M.; Trewhella, J.; Cavicchioli, R.
    A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability (2010), Protein Eng. Des. Sel., 23, 769-780.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.1 purified modified enzyme TAAMOD, vapour diffusion, 10 mg/ml protein in 10 mM Tris, pH 7.5, and 5 mM CaCl2 against a solution of 20% PEG 4000, 0.4 M ammonium sulfate and 0.1 M MES, pH 7.2, 2 weeks, X-ray diffraction structure determination and analysis at 2.4 A reolution Aspergillus oryzae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information activation thermodynamics for kinetic stability of native and modified enzymes, overview Aspergillus oryzae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 additional information no requirement for Ca2+ Aspergillus oryzae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 additional information
-
 the modified enzyme TAAMOD acquires a higher molecular weight than the native enzyme TAAUM by 2096 Da Aspergillus oryzae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Aspergillus oryzae
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 commercial preparation
-
 Aspergillus oryzae
-

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 TAA
-
 Aspergillus oryzae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 40 60 assay at Aspergillus oryzae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 50
-
 at a temperature approximating the optimal temperature of 50°C, the modified enzyme TAAMOD has a 28fold higher t1/2-inact of 340 min compared with native enzyme TAAUM with 12 min Aspergillus oryzae
3.2.1.1 53
-
 t1/2 inact of the native enzyme TAAUM is 6 min, of the modified enzyme TAAMOD 140 min Aspergillus oryzae
3.2.1.1 55
-
 t1/2 inact of the native enzyme TAAUM is 4 min, of the modified enzyme TAAMOD 30 min Aspergillus oryzae
3.2.1.1 60
-
 t1/2 inact of the native enzyme TAAUM is 1 min, of the modified enzyme TAAMOD 6 min Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 5
-
-
 Aspergillus oryzae

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.1 Aspergillus oryzae the modified enzyme TAAMOD acquires a higher pI than the native enzyme TAAUM
-
 additional information

General Information

EC Number General Information Comment Organism
3.2.1.1 additional information enzyme modification using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride in the presence of a nucleophile, AME, to activate the carboxyl groups of the enzyme, comparisons in anion and cation exchange chromatographies and by native PAGE, overview. The modifications project into the bulk solvent. The enhanced thermostability leads to increased productivity Aspergillus oryzae