ArticleCurrent microbiology2020
Identification and Characterization of the Small Heat Shock Protein Hsp20 from Oenococcus oeni SD-2a.
Article in Current microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 9 citations in OpenAlex.
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- Whole-Genome Sequencing of Extended-Spectrum β-Lactamase-ProducingPathogens (Basel, Switzerland) · 2025Article
- Gene manipulation inFrontiers in microbiology · 2025Article
- Effects of small heat shock proteins from thermotolerant bacteria on the stress resistance of Escherichia coli to temperature, pH, and hyperosmolarity.Extremophiles : life under extreme conditions · 2024Article
- Analysis of Transcriptomic Response to SOMicrobiology spectrum · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Oenococcus oeni can exert its function in hostile wine conditions during the malolactic fermentation process. Therefore, it is an important microbial resource for exploring resistance genes. Hsp20 is an important small heat shock protein from O. oeni. The conserved consensus motif "A-x-x-x-x-G-x-L" of Hsp20 announced its role as a member of the small heat shock protein family. The hsp20 gene from O. oeni SD-2a was cloned to create the recombinant plasmid pTriEx-Hsp20. The recombinant plasmid was transformed into Escherichia coli BL21(DE3) competent cells, and the Hsp20 protein was induced by isopropyl-β-D-thiogalactoside (IPTG). The hsp20 gene from O. oeni SD-2a was successfully expressed, and a 20-kDa fusion protein was identified by SDS-PAGE. The purified Hsp20 protein was obtained using Ni-affinity chromatography. Additionally, BL21(DE3)/Hsp20 and BL21(DE3)/Ctrl were treated at high temperatures of 42 and 52 °C, at pH values of 2.0-12.0, under oxidative shock with 0.1% (v/v) and 0.2% (v/v) H
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