ArticleApplied and environmental microbiology2015
A chlorogenic acid esterase with a unique substrate specificity from Ustilago maydis.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- Analysis of the Atypical Temperature Dependence and Conformational Changes During Turnover of a Lactobacillus Chlorogenic Acid Esterase.Biochemistry · 2026Article
- Uncovering enzymatic tools promoting lignocellulose breakdown in the anaerobic bacterium Ruminiclostridium cellulolyticum.Communications biology · 2025Article
- AI-integrated metabolomics maps functional divergence of microbial consortia in field-grown maize.Plant cell reports · 2025Article
- Identification of the first plant caffeoyl-quinate esterases inFrontiers in plant science · 2025Article
- Huitlacoche (Molecules (Basel, Switzerland) · 2023Review
- A novel esterase from a soil metagenomic library displaying a broad substrate range.AMB Express · 2021Article
- Feruloyl Esterases for Biorefineries: Subfamily Classified Specificity for Natural Substrates.Frontiers in bioengineering and biotechnology · 2020Article
- New Insights of Ustilago maydis as Yeast Model for Genetic and Biotechnological Research: A Review.Current microbiology · 2019Review
- A type D ferulic acid esterase from Streptomyces werraensis affects the volume of wheat dough pastries.Applied microbiology and biotechnology · 2018Article
- Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications.Biotechnology for biofuels · 2016Review
- Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses.Veterinary research · 2015Review
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Authors and funding
7 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
An extracellular chlorogenic acid esterase from Ustilago maydis (UmChlE) was purified to homogeneity by using three separation steps, including anion-exchange chromatography on a Q Sepharose FF column, preparative isoelectric focusing (IEF), and, finally, a combination of affinity chromatography and hydrophobic interaction chromatography on polyamide. SDS-PAGE analysis suggested a monomeric protein of ∼71 kDa. The purified enzyme showed maximal activity at pH 7.5 and at 37°C and was active over a wide pH range (3.5 to 9.5). Previously described chlorogenic acid esterases exhibited a comparable affinity for chlorogenic acid, but the enzyme from Ustilago was also active on typical feruloyl esterase substrates. Kinetic constants for chlorogenic acid, methyl p-coumarate, methyl caffeate, and methyl ferulate were as follows: Km values of 19.6 μM, 64.1 μM, 72.5 μM, and 101.8 μM, respectively, and kcat/Km values of 25.83 mM(-1) s(-1), 7.63 mM(-1) s(-1), 3.83 mM(-1) s(-1) and 3.75 mM(-1) s(-1), respectively. UmChlE released ferulic, p-coumaric, and caffeic acids from natural substrates such as destarched wheat bran (DSWB) and coffee pulp (CP), confirming activity on complex plant biomass. The full-length gene encoding UmChlE consisted of 1,758 bp, corresponding to a protein of 585 amino acids, and was functionally produced in Pichia pastoris GS115. Sequence alignments with annotated chlorogenic acid and feruloyl esterases underlined the uniqueness of this enzyme.
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