<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>8(1)</volume><submitter>Biundo A</submitter><pubmed_abstract>The activity of the esterase (Cbotu_EstA) from Clostridium botulinum on the polyester poly(ethylene terephthalate) (PET) was improved by concomitant engineering of two different domains. On the one hand, the zinc-binding domain present in Cbotu_EstA was subjected to site-directed mutagenesis. On the other hand, a specific domain consisting of 71 amino acids at the N-terminus of the enzyme was deleted. Interestingly, a combination of substitution of residues present in the zinc-binding domain (e.g. S199A) synergistically increased the activity of the enzyme on PET seven fold when combined to the truncation of 71 amino acids at the N-terminus of the enzyme only. Overall, when compared to the native enzyme, the combination of truncation and substitutions in the zinc-binding domain lead to a 5</pubmed_abstract><journal>Scientific reports</journal><pagination>3745</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5829244</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Synergistic effect of mutagenesis and truncation to improve a polyesterase from Clostridium botulinum for polyester hydrolysis.</pubmed_title><pmcid>PMC5829244</pmcid><pubmed_authors>Guebitz GM</pubmed_authors><pubmed_authors>Ribitsch D</pubmed_authors><pubmed_authors>Reich J</pubmed_authors><pubmed_authors>Biundo A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Synergistic effect of mutagenesis and truncation to improve a polyesterase from Clostridium botulinum for polyester hydrolysis.</name><description>The activity of the esterase (Cbotu_EstA) from Clostridium botulinum on the polyester poly(ethylene terephthalate) (PET) was improved by concomitant engineering of two different domains. On the one hand, the zinc-binding domain present in Cbotu_EstA was subjected to site-directed mutagenesis. On the other hand, a specific domain consisting of 71 amino acids at the N-terminus of the enzyme was deleted. Interestingly, a combination of substitution of residues present in the zinc-binding domain (e.g. S199A) synergistically increased the activity of the enzyme on PET seven fold when combined to the truncation of 71 amino acids at the N-terminus of the enzyme only. Overall, when compared to the native enzyme, the combination of truncation and substitutions in the zinc-binding domain lead to a 5</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Feb</publication><modification>2026-04-30T09:33:29.43Z</modification><creation>2019-03-26T23:04:59Z</creation></dates><accession>S-EPMC5829244</accession><cross_references><pubmed>29487314</pubmed><doi>10.1038/s41598-018-21825-9</doi></cross_references></HashMap>