Many research reports have indicated that single enzyme products are less effective than multi-enzyme products. Naturally complex substrates occurring in feed are more effectively degraded with a host of synergistic enzymes than a single enzyme targeting a specific bond type. Many enzyme companies attempt to mix purified enzyme sources to achieve this effect. Naturally it is impossible to predict which combination will be optimal given the complexity and variation in animal feed. An alternative approach employed by GNC Bioferm is to rely on substrate sources in the fermentation process that are representative of the target materials in feed. Basically, the production organism is forced to produce a viable enzyme complement to survive in a highly competitive environment. A few of the secondary enzyme activities that occur in addition to guaranteed activities in GNC Bioferm products are as follows: 1. Cellulolytic enzymes refer to the enzyme system responsible for the degradation of cellulose. This system includes: Endo-1,4-β -glucanase (carboxymethylcellulase) which degrades linear β - 1,4-glucans; Exo-1,4-β -glucanase which releases oligosaccharides from amorphous cellulose; Exo-cellobiohydrolase which releases cellobiose from cellulose and oligosaccharides; β -glucosidase which releases glucose from oligosaccharides; and cellobiase, which releases glucose from the disaccharide cellobiose. 2. Hemicellulolytic enzymes refers to the multiple enzyme system that degrades linear β-1,4-xylan to xylose. The primary enzyme requirement is endo-xylanase, which is assisted by β-xylosidase that releases xylose from xylo-oligosaccharides. Arabinosidase enzyme releases arabinose from branched xylan thus exposing the xylan ‘backbone’ to subsequent attack. Ferulic acid esterase similarly assists by releasing xylan from the lignified cell wall core. 3. α-Galactosidase releases galactose from the oligosaccharides raffinose, stachyose, and verbascose occurring in most plant protein sources such as soybean meal, lupins, peas, and canola meal. Galactomannase degrades cell wall elements based on mannose. Secondary enzymes act in concert with a variety of poorly understood factors which assist enzymes in binding to their respective substrates are critical for the degradation of intact materials. As an example, the following graph represents the degradation of the carbohydrate fraction of soybean meal using Endofeed or competitor products, monitored by reducing sugar release.  Naturally, the capacity to degrade intact feed materials as opposed to purified substrates more closely represents the gastrointestinal environment in which feed enzymes must function. Much of the research with feed enzymes has focused on the elimination of high intestinal viscosity imposed by solubilized fiber fractions occurring in cereal grains. A second benefit, albeit quantitatively less important than viscosity reduction, is the destruction of cell walls which encapsulate important nutrients thus hindering exposure to digestive (or exogenous) enzymes. This effect can be demonstrated with dietary phytase, which releases phosphorus from phytic acid, the organic form of phosphorus found in plant materials, especially oilseed meals.  Aside from secondary enzyme activities, binding factors that facilitate binding of the enzymes to their respective substrates are also credited with a role in optimizing substrate degradation. This phenomenon is demonstrated with amylases as occur in responsible for the degradation of starch. Amylase activity is normally measured for the purpose of activity declaration with gelatinized starch (solubilized by aqueous heating), which is vastly more susceptible to enzyme attack than raw starch. |
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Plant: PO Box 6, Bradwell, SK. Canada S0K 0P0
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Email: gnc.bioferm@shaw.ca
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