ArticleExtremophiles : life under extreme conditions2016
Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7.
Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 29 citations in OpenAlex.
- Expression and characterization of Est2: a novel cold-adapted esterase from Antarctic bacterium defining the new esterase family XXII.Frontiers in microbiology · 2025Article
- Whole-Genome Sequencing of a Potential Ester-Synthesizing Bacterium Isolated from Fermented Golden Pomfret and Identification of Its Lipase Encoding Genes.Foods (Basel, Switzerland) · 2022Article
- Metagenomic Screening for Lipolytic Genes Reveals an Ecology-Clustered Distribution Pattern.Frontiers in microbiology · 2022Article
- Enhancement of Monascus yellow pigments production by activating the cAMP signalling pathway in Monascus purpureus HJ11.Microbial cell factories · 2020Article
- A Novel VIII Carboxylesterase with High Hydrolytic Activity Against Ampicillin from a Soil Metagenomic Library.Molecular biotechnology · 2019Article
- Expression and characterization of a 9-cis-epoxycarotenoid dioxygenase fromBiotechnology reports (Amsterdam, Netherlands) · 2018Article
- Screening, purification, and characterization of a novel organic solvent-tolerant esterase, Lip2, from Monascus purpureus strain M7.Extremophiles : life under extreme conditions · 2017Article
- A Novel Halotolerant Thermoalkaliphilic Esterase from Marine BacteriumFrontiers in microbiology · 2017Article
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6 authors at 1 institution in 1 country.
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Abstract
Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif Gly(173)-Xaa-Ser(175)-Xaa-Gly(177) that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4-10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184-216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase.
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