Article (Scientific journals)
Isolation and cultivation of xylanolytic and cellulolytic Sarocladium kiliense and Trichoderma virens from the gut of the termite Reticulitermes santonensis
Tarayre, Cédric; Bauwens, Julien; Brasseur, Catherine et al.
2014In Environmental Science and Pollution Research
Peer Reviewed verified by ORBi
 

Files


Full Text
Tarayre et al., 2014 (3).pdf
Publisher postprint (1.21 MB)
Request a copy

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Xylanase; Cellulase; Reticulitermes santonensis; Sarocladium kiliense; Trichoderma virens
Abstract :
[en] The purpose of this work was the isolation and cultivation of cellulolytic and xylanolytic microorganisms extracted from the gut of the lower termite Reticulitermes santonensis. Microcrystalline cellulose (with and without lignin) and beech wood xylan were used as diets instead of poplar wood in order to select cellulose and hemicellulose-degrading fungi. The strain Sarocladium kiliense (Acremonium kiliense) CTGxxyl was isolated from the termites fed on xylan, while the strain Trichoderma virens CTGxAviL was isolated from the termites fed on cellulose (with and without lignin). Both molds were cultivated in liquid media containing different substrates: agro-residues or purified polymers. S. kiliense produced maximal β-glucosidase, endo-1,4-β-D-glucanase, exo-1,4-β-D-glucanase and endo-1,4-β-D-xylanase activities of 0.103, 3.99, 0.53, and 40.8 IU/ml, respectively. T. virens produced maximal β-xylosidase, endo-1,4-β-D-glucanase, exo-1,4-β-D-glucanase, and endo-1,4-β-D-xylanase activities of 0.38, 1.48, 0.69, and 426 IU/ml. The cellulase and the xylanase of S. kiliense, less common than T. virens, were further investigated. The optimal activity of the xylanase was observed at pH 9–10 at 60 °C. The cellulase showed its maximal activity at pH 10, 70 °C. Zymography identified different xylanases produced by both molds, and some fragment sizes were highlighted: 35, 100, and 170 kDa for S. kiliense and 20, 40, 80, and 170 kDa for T. virens. In both cases, endo-1,4-β-D-xylanase activitieswere confirmed through mass spectrometry.
Disciplines :
Microbiology
Biotechnology
Author, co-author :
Tarayre, Cédric ;  Université de Liège - ULiège > Chimie et bio-industries > Bio-industries
Bauwens, Julien ;  Université de Liège - ULiège > Sciences agronomiques > Entomologie fonctionnelle et évolutive
Brasseur, Catherine ;  Université de Liège - ULiège > Département de chimie (sciences) > Laboratoire de spectrométrie de masse (L.S.M.)
Mattéotti, Christel
Millet, Catherine
Guiot, Pierre Alexandre
Destain, Jacqueline ;  Université de Liège - ULiège > Chimie et bio-industries > Bio-industries
Vandenbol, Micheline ;  Université de Liège - ULiège > Chimie et bio-industries > Microbiologie et génomique
Portetelle, Daniel ;  Université de Liège - ULiège > Chimie et bio-industries > Microbiologie et génomique
De Pauw, Edwin  ;  Université de Liège - ULiège > Département de chimie (sciences) > Laboratoire de spectrométrie de masse (L.S.M.)
Haubruge, Eric  ;  Université de Liège - ULiège > Premier Vice-Recteur
Francis, Frédéric  ;  Université de Liège - ULiège > Sciences agronomiques > Entomologie fonctionnelle et évolutive
Thonart, Philippe ;  Université de Liège - ULiège > Chimie et bio-industries > Bio-industries
More authors (3 more) Less
Language :
English
Title :
Isolation and cultivation of xylanolytic and cellulolytic Sarocladium kiliense and Trichoderma virens from the gut of the termite Reticulitermes santonensis
Publication date :
October 2014
Journal title :
Environmental Science and Pollution Research
ISSN :
0944-1344
eISSN :
1614-7499
Publisher :
Springer Science & Business Media B.V.
Peer reviewed :
Peer Reviewed verified by ORBi
Name of the research project :
Termitofuel
Available on ORBi :
since 13 October 2014

Statistics


Number of views
116 (27 by ULiège)
Number of downloads
6 (6 by ULiège)

Scopus citations®
 
15
Scopus citations®
without self-citations
14
OpenCitations
 
8

Bibliography


Similar publications



Contact ORBi