Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Δημιουργός/Συγγραφέας:	Zarafeta D. Kissas D. Sayer C. Gudbergsdottir S.R. Ladoukakis E. Isupov M.N. [EL] Χατζηιωάννου, Αριστοτέλης[EN] Chatziioannou, Aristotelis Peng X. Littlechild J.A. [EL] Σκρέτας, Γιώργος[EN] Skretas, George [EL] Κολίσης, Φραγκίσκος Ν.[EN] Kolisis, Fragiskos N.‏
Εκδότης:	Public Library of Science
Ημερομηνία:	2016
Γλώσσα:	Αγγλικά
ISSN:	1932-6203
DOI:	10.1371/journal.pone.0146454
Άλλο:	PubMed ID: 26741138
Περίληψη:	With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70°C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics.
Τίτλος πηγής δημοσίευσης:	PLoS ONE
Τόμος/Κεφάλαιο:	11
Τεύχος:	1
Θεματική Κατηγορία:	[EL] Βιολογία (Γενικά)[EN] Biology (General)
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Κάτοχος πνευματικών δικαιωμάτων:	© 2016 Zarafeta et al.
Όροι και προϋποθέσεις δικαιωμάτων:	This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Σημειώσεις:	Seventh Framework Programme, FP7: 265933; Biotechnology and Biological Sciences Research Council, BBSRC: BB/L002035/1; University of Exeter. This work has been carried out in the framework of the HotZyme Project ( http://hotzyme.com , grant agreement no. 265933) financed by the European Union 7 Framework Programme FP7/2007-2013, an EU FP7 Collaborative programme that aims to use metagenomic approaches to identify new thermostable hydrolases which have improved performance and/or novel functionalities for different industrial processes from diverse hot environments.
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο