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Please use this identifier to cite or link to this item: http://hdl.handle.net/10400.5/1279

Title: Role of a family 11 carbohydrate-binding module in the function of a recombinant cellulase used to supplement a barley based diet for broiler chickens
Authors: Lordelo, M.M.
Guerreiro, C.I.P.D.
Ribeiro, T.
Ponte, P.I.P.
Falcão, L.
Freire, J.P.B.
Ferreira, L.M.A.
Prates, J.A.M.
Fontes, C.M.G.A.
Keywords: broiler chicken
carbohydrate-binding modules
cellulase
xylanase
Issue Date: 2008
Publisher: Taylor & Francis
Citation: "British Poultry Science". ISSN 0007-1668. 49:4 (2008) 446-454
Abstract: Cellulases and xylanases display a modular architecture that comprises a catalytic module linked to one or more non-catalytic carbohydrate-binding modules (CBMs). CBMs have been classified into 52 different families, based on primary structure similarity. These non-catalytic modules mediate a prolonged and intimate contact of the enzyme with the target substrate eliciting efficient hydrolysis of the target polysaccharides. 2. A study was undertaken to investigate the importance of a family 11 CBM, displaying high affinities for barley -glucans, in the function of recombinant derivatives of cellulase CtLic26A-Cel5E of Clostridium thermocellum used to supplement a barley-based diet for broiler chicken. 3. The results showed that birds fed on diets containing the recombinant CtLic26A-Cel5E modular derivatives or the commercial enzyme mixture RovabioTM Excel AP displayed improved performance when compared with birds fed on diets not supplemented with exogenous enzymes. 4. It is suggested that the enzyme dosage used in this study (30 U/kg of basal diet), was probably too high for the efficacy of the family 11 CBM to be noticed. It remains to be established if the targeting effect resulting from the incorporation of CBMs in plant cell wall hydrolases may be effective at lower exogenous enzyme dosages.
URI: http://hdl.handle.net/10400.5/1279
ISSN: 0007-1668
Appears in Collections:DPAA - Artigos de Revistas

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