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Fig. 1 | Microbial Cell Factories

Fig. 1

From: Development of a whole-cell biocatalyst for diisobutyl phthalate degradation by functional display of a carboxylesterase on the surface of Escherichia coli

Fig. 1

Multiple sequence alignment between CarEW and some previously reported esterases with PAEs biodegradation capacities. Sequences retrieved from the NCBI database and were aligned by CLUSTAL W and were rendered using ESPript output. Sequences are grouped according to similarity. Esterase with a known three-dimensional structure (PDB: 1QE3) from Bacillus subtilis; KMW28714.1, Carboxylesterase from Sphingobium yanoikuyae; AGY55960.1, DphB from metagenomics library; AEW03609.1, EstS1 from Sulfobacillus acidophilus DSM 10332; AFK31309.1, PE-hydrolase from Acinetobacter sp. M673; WP_023629646.1, alpha/beta hydrolase from Pseudomonas mosselii; ABH00399.1, PatE from Rhodococcus jostii RHA1. Conserved amino acids are highlighted in a yellow font on a white background. The analysis revealed the presence of tripeptide HGG (red dots on top of the sequences) and PVMVW (underline in red) in most of test strains. Symbols above sequences represent the secondary structure, springs represent helices, and arrows represent β-strands

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