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https://hdl.handle.net/10442/17447
Εξειδίκευση τύπου : | Άρθρο σε επιστημονικό περιοδικό |
Τίτλος: | Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
Δημιουργός/Συγγραφέας: | Zarafeta D. Moschidi D. Ladoukakis E. Gavrilov S. [EL] Χρυσίνα, Ευαγγελία Δ.[EN] Chrysina, Evangelia D. [EL] Χατζηιωάννου, Αριστοτέλης[EN] Chatziioannou, Aristotelis Kublanov I. [EL] Σκρέτας, Γιώργος[EN] Skretas, George [EL] Κολίσης, Φραγκίσκος Ν.[EN] Kolisis, Fragiskos N. |
Εκδότης: | Nature Publishing Group |
Ημερομηνία: | 2016 |
Γλώσσα: | Αγγλικά |
ISSN: | 2045-2322 |
DOI: | 10.1038/srep38886 |
Άλλο: | PubMed ID: 27991516 |
Περίληψη: | Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Here, we have identified a new esterolytic enzyme by screening a metagenomic sample collected from a hot spring in Kamchatka, Russia. Biochemical characterization of the new esterase, termed EstDZ2, revealed that it is highly active against medium chain fatty acid esters at temperatures between 25 and 60 °C and at pH values 7-8. The new enzyme is moderately thermostable with a half-life of more than six hours at 60 °C, but exhibits exquisite stability against high concentrations of organic solvents. Phylogenetic analysis indicated that EstDZ2 is likely an Acetothermia enzyme that belongs to a new family of bacterial esterases, for which we propose the index XV. One distinctive feature of this new family, is the presence of a conserved GHSAG catalytic motif. Multiple sequence alignment, coupled with computational modelling of the three-dimensional structure of EstDZ2, revealed that the enzyme lacks the largest part of the "cap" domain, whose extended structure is characteristic for the closely related Family IV esterases. Thus, EstDZ2 appears to be distinct from known related esterolytic enzymes, both in terms of sequence characteristics, as well as in terms of three-dimensional structure. |
Τίτλος πηγής δημοσίευσης: | Scientific Reports |
Τόμος/Κεφάλαιο: | 6 |
Θεματική Κατηγορία: | [EL] Βιολογία (Γενικά)[EN] Biology (General) [EL] Χημεία (Γενικά)[EN] Chemistry (General) |
Αξιολόγηση από ομότιμους (peer reviewed): | Ναι |
Κάτοχος πνευματικών δικαιωμάτων: | © The Author(s) 2016. |
Όροι και προϋποθέσεις δικαιωμάτων: | All Open Access, Gold, Green |
Σημειώσεις: | Seventh Framework Programme, FP7: 265933; State Scholarships Foundation, IKY; European Social Fund, ESF. Additional support was also provided by the Synthetic Biology research infrastructure OMIC-ENGINE, financed by the Hellenic General Secretariat of Research and Technology and the National Strategic Reference Framework (NSRF). DZ is the recipient of a PhD fellowship from the Greek State Scholarships Foundation (Idryma Kratikon Ypotrofion-IKY) in the framework of the Research Grant Excellence IKY-Siemens Program, which is co-financed by the European Social Fund and the Greek Government. |
Εμφανίζεται στις συλλογές: | Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο
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