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Growth and carcass performance in broiler chickens supplemented with beta-glucanase from aerobic fungi Aspergilus niger and Trichoderma longibrachiatum

Mottaghitalab, M., Ebrahimiyan, M.R.
J. poult. sci 2007 v.44 no.4 pp. 383-388
broiler chickens, animal growth, animal performance, carcass quality, dietary supplements, beta-glucanase, Aspergillus niger, Hypocrea jecorina, feed conversion, barley, enzyme activity, Bacillus subtilis, experimental diets, enzymatic hydrolysis
A variety of factors can affect feed efficiency in poultry; among them is beta-Glucan. beta-Glucan in feeds is often poorly digest and has deleterious effects on nutrient absorption. Supplementation of diets with proper enzyme can enhance nutrient digestion and absorption. The aim of this study was beta-Glucanase production from Aspergillus niger and Trichoderma longibrachiatum (GPbeta-Glucanase), as well as its in vitro and in vivo assessment. Yeast biomass was produced using Zapek medium with Glucose and inoculated in Erlenmeyer flasks (repressed conditions) with above fungi. The mycelia then transferred to Erlenmeyer flasks containing Zapek medium supplemented with 2% barely beta-Glucan and incubated (induction conditions), and enzyme recovered from the medium. The mean activities of GPbeta-Glucanase and commercial beta-Glucanase from Bacillus subtillis (ZYbeta-Glucanase) were recorded as 1348 +/- 5.12 and 1251 +/- 5.31 BGU1/g respectively. Chick model was used for in vivo assessment. 540 Broiler chicks were fed one of nine diets in a 3 x 3 factorial arrangement from 1 to 49 days of age. The factors were: enzyme addition (0, ZYbeta-Glucanase and GPbeta-Glucanase) and level of hull-less barley (HB) in diet (0, 40, and 60%). The results showed that supplementation of diets containing 40% HB either with commercial or produced enzyme led to significant (P<0.05) increase in weight gain and feed intake, whereas significant (P<0.05) decrease feed efficiency, however no significant differences were observed between two kinds of enzyme. Conclusion was that GPbeta-Glucanase is of great potential and comparable to ZYbeta-Glucanase for beta-Glucan hydrolysis.