FN Archimer Export Format
PT J
TI Functional Screening of Hydrolytic Activities Reveals an Extremely Thermostable Cellulase from a Deep-Sea Archaeon
BT 
AF Leis, Benedikt
   Heinze, Simon
   Angelov, Angel
   Pham, Vu Thuy Trang
   Thürmer, Andrea
   Jebbar, Mohamed
   Golyshin, Peter N.
   Streit, Wolfgang R.
   Daniel, Rolf
   Liebl, Wolfgang
AS 1:1;2:1;3:1;4:1;5:2;6:3;7:4;8:5;9:2;10:1;
FF 1:;2:;3:;4:;5:;6:;7:;8:;9:;10:;
C1 Department of Microbiology, School of Life Sciences Weihenstephan, Technische Universität München, Freising- Weihenstephan, German
   Göttingen Genomics Laboratory, Department of Genomic and Applied Microbiology, Georg- August University Göttingen, Göttingen, Germany
   Laboratoire de Microbiologie des Environnements Extrêmes-UMR 6197 (CNRS-Ifremer-UBO), Institut Universitaire Européen de la Mer, Université de Bretagne Occidentale, Plouzané, France
   School of Biological Sciences, Bangor University, Bangor, UK
   Fakultät für Mathematik, Informatik und Naturwissenschaften Biologie, Biozentrum Klein Flottbek, Universität Hamburg, Hamburg, Germany
C2 UNIV MUNCHEN, GERMAN
   UNIV GOTTINGEN, GERMANY
   UBO, FRANCE
   UNIV BANGOR, UK
   UNIV HAMBURG, GERMANY
UM BEEP-LM2E
IN DOAJ
IF 5.122
TC 23
UR https://archimer.ifremer.fr/doc/00601/71319/69744.pdf
   https://archimer.ifremer.fr/doc/00601/71319/69745.pdf
   https://archimer.ifremer.fr/doc/00601/71319/69746.pdf
LA English
DT Article
DE ;functional screenings;extreme thermostable protein;archaeal endoglucanase;enzymatic characterization
AB Extreme habitats serve as a source of enzymes that are active under extreme conditions and are candidates for industrial applications. In this work, six large-insert mixed genomic libraries were screened for hydrolase activities in a broad temperature range (8–70°C). Among a variety of hydrolytic activities, one fosmid clone, derived from a library of pooled isolates of hyperthermophilic archaea from deep sea vents, displayed hydrolytic activity on carboxymethyl cellulose substrate plates at 70°C but not at lower temperatures. Sequence analysis of the fosmid insert revealed a gene encoding a novel glycoside hydrolase family 12 (GHF12) endo-1,4-β-glucanase, termed Cel12E. The enzyme shares 45% sequence identity with a protein from the archaeon Thermococcus sp. AM4 and displays a unique multidomain architecture. Biochemical characterization of Cel12E revealed a remarkably thermostable protein, which appears to be of archaeal origin. The enzyme displayed maximum activity at 92°C and was active on a variety of linear 1,4-β-glucans like carboxymethyl cellulose, β-glucan, lichenan, and phosphoric acid swollen cellulose. The protein is able to bind to various insoluble β-glucans. Product pattern analysis indicated that Cel12E is an endo-cleaving β-glucanase. Cel12E expands the toolbox of hyperthermostable archaeal cellulases with biotechnological potential. 
PY 2015
PD JUN
SO Frontiers in Bioengineering and Biotechnology
SN 2296-4185
PU Frontiers Media SA
VL 3
IS 95
UT 000536548500092
DI 10.3389/fbioe.2015.00095
ID 71319
ER

EF