Literature summary for 3.2.1.1 extracted from

Shaw, A.; Bott, R.; Day, A.G.
Protein engineering of alpha-amylase for low pH performance (1999), Curr. Opin. Biotechnol., 10, 349-352.

Search for more literature for 3.2.1.1

Application

Application	Comment	Organism
synthesis	industrial-scale starch liquefaction	Bacillus licheniformis

Protein Variants

Protein Variants	Comment	Organism
A209V	more thermostable than wild type enzyme	Bacillus licheniformis
H133Y	more thermostable than wild type enzyme	Bacillus licheniformis
M15T/H133Y/N188S	at pH 83°C, pH 5.0, 5 mM CaCl2, 4fold longer half-life than wild-type enzyme	Bacillus licheniformis
M15T/H133Y/N188S/A209V	at pH 83°C, pH 5.0, 5 mM CaCl2, 23fold longer half-life than wild-type enzyme	Bacillus licheniformis
M15T/N188S	at pH 83°C, pH 5.0, 5 mM CaCl2, 1.5fold longer half-life than wild-type enzyme	Bacillus licheniformis
M15T/N188S/A209V	at pH 83°C, pH 5.0, 5 mM CaCl2, 4.5fold longer half-life than wild-type enzyme	Bacillus licheniformis
additional information	engineering of the enzyme for improved industrial performance	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	P06278	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)