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Literature summary for 3.2.1.1 extracted from

  • Parashar, D.; Satyanarayana, T.
    Production of chimeric acidic alpha-amylase by the recombinant Pichia pastoris and its applications (2017), Front. Microbiol., 8, 493 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of chimeric acidic alpha-amylase Ba-Gt-amy in Pichia pastoris strain X33, real-time RT-PCR enzyme expression analysis Geobacillus thermoleovorans
recombinant expression of chimeric acidic alpha-amylase Ba-Gt-amy in Pichia pastoris strain X33, real-time RT-PCR enzyme expression analysis Bacillus acidicola

Protein Variants

Protein Variants Comment Organism
additional information construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans. Generation of multi-copy integrants that can secrete high levels of heterologous protein using multiple transformation approach followed by post-transformational vector amplification (PTVA). Method evaluation and optimization Geobacillus thermoleovorans
additional information construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans. Generation of multi-copy integrants that can secrete high levels of heterologous protein using multiple transformation approach followed by post-transformational vector amplification (PTVA). Method evaluation and optimization Bacillus acidicola

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km for raw starch is 0.79 mg/ml Geobacillus thermoleovorans
additional information
-
additional information Km for raw starch is 0.79 mg/ml Bacillus acidicola

Organism

Organism UniProt Comment Textmining
Bacillus acidicola
-
-
-
Geobacillus thermoleovorans J9PXA2
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein recombinant chimeric amylase Ba-Gt-amy is glycosylated, it has 6 N- and 6 O-glycosylation sites Geobacillus thermoleovorans
glycoprotein recombinant chimeric amylase Ba-Gt-amy is glycosylated, it has 6 N- and 6 O-glycosylation sites Bacillus acidicola

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
raw starch + H2O
-
Geobacillus thermoleovorans ?
-
?
raw starch + H2O
-
Bacillus acidicola ?
-
?

Synonyms

Synonyms Comment Organism
acidic amylase
-
Geobacillus thermoleovorans
acidic amylase
-
Bacillus acidicola

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
recombinant chimeric acidic alpha-amylase Ba-Gt-amy Geobacillus thermoleovorans
60
-
recombinant chimeric acidic alpha-amylase Ba-Gt-amy Bacillus acidicola

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, T1/2 is 40 min Geobacillus thermoleovorans
70
-
purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, T1/2 is 40 min Bacillus acidicola

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
40000
-
raw starch pH 4.0, 60°C, recombinant chimeric acidic alpha-amylase Ba-Gt-amy Geobacillus thermoleovorans
40000
-
raw starch pH 4.0, 60°C, recombinant chimeric acidic alpha-amylase Ba-Gt-amy Bacillus acidicola

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
recombinant chimeric acidic alpha-amylase Ba-Gt-amy Geobacillus thermoleovorans
4
-
recombinant chimeric acidic alpha-amylase Ba-Gt-amy Bacillus acidicola

pH Range

pH Minimum pH Maximum Comment Organism
3 6 activity range Geobacillus thermoleovorans
3 6 activity range Bacillus acidicola