New Feed Enzyme Development - The Poultry Federation

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September 2009, ChemGen Corp.The high molecular weight sugar polymer extracted from DDGS was compared to a similar extract frombrewers dry yeast after digestion with purified β‐1,3‐glucanase in Figure 17. The fragmentation patternis similar to the yeast extract as would be expected. Soy hull extract hydrolyzed with the purified β‐1,3‐glucanase has a slightly different pattern without a dp 5 fragment. An extract from soy concentrate, aprotein enriched had much reduced glucanase substrate.Figure 17 – Carbohydrate gel analysis of the fragmentation of soy hull, DDGS and dried yeast waterextracts with purified β‐1,3‐glucanaseCarbohydrate gel as described inFigure 7 modified with higher %gel.Gel Lanes1‐glucose2‐ maltose3‐maltotriose4‐ maltodextrin dp 4‐10(dp 7‐10 not resolved)5‐ soy concentrate extract6 –soy hull extract7,8 – DDGS extract9 ‐dried brewer’s yeast extract32% acrylamine gel, 2 hours, 200 VLanes 5‐9 digested with purifiedβ‐1,3‐glucanaseMore work is needed to understand the β‐1,3‐glucan content in feed components to decide thebest applications of the new enzyme. Products with high yeast content are the area of currentfocus. Table 6 shows the glucan content from several additional raw materials including theDDGSIt is very clear that the β‐1,3‐glucan is a strong PAMP and that it is found in feed from manypossible sources. Animal testing data provided below shows that a broiler 21 day chicken cagescreening test lowered AGP similar to the observation with mannanase. This was followed bylarger growth tests showing that the addition of ChemGen’s novel source of β‐1,3‐glucanasecan, in some cases, significantly improve the growth performance benefit of Hemicell®. Thedegree of the added benefit has ranged from very large to moderate, and the current theory isthat the difference likely relates to the β‐1,3‐glucan content in feed that was not defined ininitial experiments.D.M. Anderson and H. Hsiao, New Feed Enzymes Page 20
September 2009, ChemGen Corp.Table 6 – β‐1,3‐glucan content of DDGS and yeast feed products% DDGS DDGS Brewers BDG BDG BDG MDGTotalmannoseAvg. 15samplesUSAmidwestDryYeast0.97 0.843 6.17China-1 China-2 Philippines ChinaSolublemannoseTotalglucoseSolubleglucoseβ‐1,3‐Glucan0.561 0.322 2.0095.918 7.873 6.1792.512 4.62 1.3340.298 0.525 3.814 1.02 0.79 0.5 1.012Testing β‐1,3‐glucanase in Feeding ExperimentsThe enzyme β‐1,3‐glucanase actually already exists in Hemicell®, but at a low level. The β‐1,3‐glucanaseexpression level in the Hemicell production strain was increased to a commercially useful level toprovide a safe supply from a host that does not contain any foreign DNA sequences. This feed‐approvedmicrobial strain also naturally produces a number of other potentially useful enzymes for feed that weplan to exploit. The new strain produces β‐mannanase and the β‐1,3‐glucanase simultaneously. Thetarget dose for the β‐1,3‐glucanase like Hemicell® mannanase has been 70 to 100 MU/ton (ChemGenUnits).The new enzyme will be sold in combination with mannanase, but in some trials it was tested separatelyin a more purified form. Initially a 21 day cage trial was performed at Southern Poultry Research asdescribed in Table 7. The WAFC was significantly improved in the short 21 day test, and AGP wassignificantly reduced over control. This early result indicated that further testing and development of β‐1,3‐glucanse as a feed enzyme was warranted.In the first pen trial shown below was a 42 day turkey hen experiment comparing β‐1,3‐glucanse to acontrol, and Hemicell® and β‐1,3‐glucanse plus Hemicell®. This trial used a commercial type corn‐soydiet and feed was produced at a commercial mill. The results in Table 8 showed that this form of β‐1,3‐glucanase significantly reduced the AGP (again looking at AGP in a sub population of 30 birds only) butadding the combination of mannanase and glucanase did not reduce AGP further. The β‐1,3‐glucanasealso significantly improved the feed conversion over the control. Unlike the AGP result, the growthperformance was significantly better when the enzymes were combined. The Hemicell® and β-1,3-glucanase + Hemicell ® data is the average of two separate treatments in each case for a very highdegree of replication.D.M. Anderson and H. Hsiao, New Feed Enzymes Page 21
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