Ontology highlight
ABSTRACT:
SUBMITTER: Zhang XY
PROVIDER: S-EPMC4249001 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Applied and environmental microbiology 20140822 22
EstS1, a newly identified thermostable esterase from Sulfobacillus acidophilus DSM10332, was heterologously expressed in Escherichia coli and shown to enzymatically degrade phthalate esters (PAEs) to their corresponding monoalkyl PAEs. The optimal pH and temperature of the esterase were found to be 8.0 and 70°C, respectively. The half-life of EstS1 at 60°C was 15 h, indicating that the enzyme had good thermostability. The specificity constant (kcat/Km) of the enzyme for p-nitrophenyl butyrate wa ...[more]