ORBi: Berlemont Renaud - Insights into the metagenomic approach : identification and characterization of cellulases involved in bacterial cellulose synthesis

Reference : Insights into the metagenomic approach : identification and characterization of cellulas...


	Document type :	Scientific congresses and symposiums : Unpublished conference
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/95402

Title :	Insights into the metagenomic approach : identification and characterization of cellulases involved in bacterial cellulose synthesis
Language :	English
Author, co-author :	Berlemont, Renaud [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
	Delsaute, Maud [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
	Galleni, Moreno [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
Publication date :	22-Mar-2010
On invitation :	Yes
Audience :	International
Event name :	239th American Chemical Society National Meeting & Exposition
Event date :	21-25/3/2010
Event organizer :	American Chemical Society
Event place (city) :	San Francisco
Event country :	USA, Ca
Keywords :	[en] cellulose ; metagenomic
Abstract :	[en] the mining of an Antarctic soil sample by functional metagenomics allowed the isolation of a cold-adapted protein (RBcel1) that hydrolyzes only carboxymethyl cellulose. The new enzyme is related to family 5 of the glycosyl hydrolase (GH5) protein from Pseudomonas stutzeri (Pst_2494) and does not possess a carbohydrate-binding domain. The protein was produced and purified to homogeneity. RBcel1 displayed an endoglucanase activity, producing cellobiose and cellotriose, using carboxymethyl cellulose as a substrate. Moreover, the study of pH and the thermal dependence of the hydrolytic activity shows that RBcel1 was active from pH 6 to pH 9 and remained significantly active when temperature decreased (18% of activity at 10 1C). It is interesting that RBcel1 was able to synthetize non-reticulated cellulose using cellobiose as a substrate. Moreover, by a combination of bioinformatics and enzyme analysis, the physiological relevance of the RBcel1 protein and its mesophilic homologous Pst_2494 protein from P. stutzeri, A1501, was established as the key enzymes involved in the production of cellulose by bacteria. In addition, RBcel1 and Pst_2494 are the two primary enzymes belonging to the GH5 family involved in this process.
Research units :	Centre d'Ingénierie des Protéines - CIP
Funders :	ACS
Name of the research project :	GeneHunt
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/95402

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