New Feed Enzyme Development - The Poultry Federation

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September 2009, ChemGen Corp.randomized complete block design (RCBD) of mixed gender pens, stratified by litter source and initialweight, into three (3) study treatments. There were ten (10) replicates per treatment, two (2) perroom. Dietary treatments included: Negative Control and the Negative Control diet profile plus enzymefor treatments (Hemicell® β‐mannanase or Hemicell® β‐mannanase + β‐1,3 ‐glucanase at two levels).Diet formulations were changed every three weeks with DDGS concentration increasing from 15% to20% and 25%. Data analysis is still in progress and the data will be published independently. However,indications from early time points show β‐1,3‐ glucanase providing significant improvement over the noenzyme and Hemicell® controls. (Jon Ferrel, personal communication).CONCLUSIONSThe innate immune system has been highly conserved through evolution with analogous elementsfound from insects, to plants to humans. Indeed, β‐1,3‐glucans elicit an evolutionarily conserved innateimmune response most likely due to its almost universal inclusion in fungal cell walls. The innateimmune system with its powerful and rapid response is essential for survival due to its role to fightinfections prior to the development of adaptive immunity in animals. However, it is a two edged sword.Analogous to the problem of the unwanted autoimmune diseases occasionally caused by faultyregulation of the adaptive immune system, we are learning that the innate immune system reacts in acounterproductive way against non‐pathogen food components that happen to be analogues of PAMPs.As more is learned about the immune systems and related scavenger systems, there should be moreopportunities to use enzymes to degrade PAMPs and PAMP analogues that are not actually pathogenassociatedin order to reduce the inflammation that they cause. We believe that this will furtherimprove feeding efficiency and animal health. Mannanase and a novel β‐1,3‐glucanase are the first twoexamples of several possible new and useful catalysts in animal feed. A third enzyme ChemGen has indevelopment looks very promising and was selected using the same model. ChemGen believes thattaking advantage of biotechnology to produce useful quantities of new feed enzymes of this category isa cost effective and efficient way to make improvements in meat and egg production.D.M. Anderson and H. Hsiao, New Feed Enzymes Page 26
September 2009, ChemGen Corp.REFERENCES1. AAFCO, 2009 Official Publication of the Association of American Feed Control Officials, Inc., P.O.PP 358‐363, 100 th Anniversary Edition, Box 478, Oxford, IN 47971, ISBN 1‐878341‐21‐92. Anderson, J.O. and R.E. Warnick (1964) Value of enzyme supplements in rations containingcertain legume seed meals or gums. Poultry Science 43: 1091‐1097.3. Vohra, P. and F.H. Kratzer (1964) The use of guar meal in chicken rations. Poultry Science 43:502‐503.4. Vohra, P. and F.H. Kratzer (1965) Improvement of guar meal by enzymes. Poultry Science 44:1201‐1205.5. Couch, J.R., Y.K. Bakshi, T.M. Ferguson, E.B. Smith and C.R. Creger (1967) The effect ofprocessing on the nutritional value of guar meal for broiler chicks. British Poultry Science 8: 243‐250.6. Verma, S.V.S. and J.M. McNab (1982) Guar meal in diets for broiler chickens. British PoultryScience 23: 95‐105.7. Ray, S., M.H. Pubolos and J. McGinnis (1982) The effect of a purified guar degrading enzyme onchicken growth. Poultry Science 61: 488‐494.8. Patel, M.B. and J. McGinnis (1985) The effect of autoclaving and enzyme supplementation ofguar meal on the performance of chicks and laying hens. Poultry Science 64: 1148‐1156.9. Nagpal, M.L., O.P. Agrawal and I.S.Bhatia (1971) Chemical and biological examination of guarmeal(Cyamopsis tetragonoloba L.) Indian J. Anim. Sci. 41: 283‐293.10. Medzhitov, R., and C.A. Janeway Jr. (2000) Inate immune recognition: mechanisms andpathways. Immunol. Rev. 173: 89‐97.11. Stahl, P.D. and R.A. Ezekowitz (1998) The mannose receptor is a pattern recognition receptorinvolved in host defence. Curr. Opin. Immunol. 10 : 50‐55.12. Eddie Ip, W. K., K. Takahashi, A.R. Ezekowitz, L.M. Stuart. (2009) Mannose‐binding lectin andinnate immunity. Immunological Reviews 230 (1): 9‐21.13. Willment, J.A. and G.D. Brown (2008) C‐Type lectin receptors in antifungal immunity. Trends inMicrobiology 16(1): 27‐32.14. Murata, H., N. Shimada and M. Yoshioka (2004) Current research on acute phase proteins inveterinary diagnosis: an overview. The Veterinary Journal 168 (1): 28‐40.15. Anderson, D.M, H. Hsiao and N.M. Dale (2009) Identification of an inflammatory compound forchicks in soybean meal – II. International Scientific Forum, Concurrent Meeting of: The southernPoultry Society, 30 th Annual Meeting; The Southern Conference on Avian Diseases, 50 th AnnualMeeting, January 26‐27, Georgia World Congress Center, Atlanta, GA.16. Anderson, D. and H. Hsiao (2006) Effect of β‐mannan (Hemicell® feed enzyme) on acute phaseprotein levels in chickens and turkeys. Abstract 231, Poultry Science Association, 95 th AnnualMeeting, July 16‐19, University of Alberta, Edmonton, AL., Canada.17. Dale, N, D. Anderson and H. Hsiao (2008) Identification of an inflammatory compound for chicksin soybean meal. Abstract M83, Int. Poultry Scientific Forum , The Southern Poultry ScienceSociety 29 th Annual Meeting, The Southern Conference on Avian Diseases 49th Annual Meeting,Jan. 21‐22, World Congress Center, Atlanta, GA, USA.18. Klasing, K.C. , D..E. Laurin, R.K. Peng and D.M. Fry (1987) Immunologically mediated growthdepression in chicks: influence of feed intake, corticosterone and interleukin‐I. J. Nutrition 117:1629‐1637.19. Spurlock, M.E. (1997) Regulation of metabolism and growth during immune challenge: anoverview of cytokine function. J. Animal Science 75: 1773‐1783.D.M. Anderson and H. Hsiao, New Feed Enzymes Page 27
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