UTL Repository >
ISA - Instituto Superior de Agronomia >
DPAA - Departamento de Produção Agricola e Animal >
DPAA - Artigos de Revistas >
Please use this identifier to cite or link to this item:
|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.|
|Keywords: ||broiler chicken|
|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.|
|Appears in Collections:||DPAA - Artigos de Revistas|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.