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|Title: ||A family 11 carbohydrate binding module (CBM) improves the efficacy of a recombinant cellulase used to supplement barley-based diets for broilers at lower dosage rates|
|Authors: ||Lordelo, M.M.|
|Keywords: ||broiler chicken|
|Issue Date: ||2008|
|Publisher: ||Taylor & Francis|
|Citation: ||"British Poultry Science". ISSN 0007-1668. 49:5 (2008) 600-608|
|Abstract: ||1. Exogenous microbial -1,3-1,4-glucanases and hemicellulases contribute to improving
the nutritive value of cereals rich in soluble non-starch polysaccharides for poultry.
2. In general, plant cell wall hydrolases display a modular structure comprising a catalytic module
linked to one or more non-catalytic carbohydrate-binding modules (CBMs). Based on primary structure
similarity, CBMs have been classified in 50 different families. CBMs anchor cellulases and hemicellulases
into their target substrates, therefore eliciting efficient hydrolysis of recalcitrant polysaccharides.
3. A study was undertaken to investigate the effects of a family 11 -glucan-binding domain in the
function of recombinant derivatives of cellulase CtLic26A-Cel5E of Clostridium thermocellum that were
used to supplement a barley-based diet at lower dosage rates.
4. The results showed that birds fed on diets supplemented with the recombinant CtLic26A-Cel5E
modular derivative containing the family 11 CBM or the commercial enzyme mixture RovabioTM Excel
AP tended to display improved performance when compared to birds fed diets not supplemented with
5. It is suggested that at lower than previously reported enzyme dosage (10 U/kg vs 30 U/kg of basal
diet), the -glucan-binding domain also elicits the function of the recombinant CtLic26A-Cel5E
6. Finally, the data suggest that exogenous enzymes added to barley-based diets act primarily in the
proximal section of the gastrointestinal tract.|
|Appears in Collections:||DPAA - Artigos de Revistas|
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