Protein fractionation byproduct from canola meal for dairy cattle.

Fiber-protein is a byproduct arising from a process for fractionating high-quality protein from canola meal. The objective of this study was to evaluate the fiber-protein fraction by examining the chemical profiles, rumen degradation, and intestinal digestive characteristics and determining the nutritive value of the fiber-protein fraction as dietary components for dairy cattle in comparison with commercial canola meal and soybean meal. Available energy values were estimated based on National Research Council guidelines, whereas total true protein content potentially absorbable in the small intestine (DVE) were predicted using the predicted DVE/degraded protein balance (OEB) model.

Transport of putrescine across duodenal, jejunal and ileal brush-border membrane of chicks (Gallus domesticus).

Luminal polyamines and their absorption are essential for proliferation of the enterocytes and, therefore, nutrition, health and development of the animal. The transport systems that facilitate the uptake of putrescine were characterized in chick duodenal, jejunal and ileal brush-border membrane vesicles prepared by MgCl2 precipitation from three-week-old chicks. An inwardly-directed Na+ gradient did not stimulate putrescine uptake and, therefore, putrescine transport in chick intestine.

Absorption of methionine and 2-hydroxy-4-methylthiobutoanic acid in conventional and germ-free chickens.

The apparent absorption of 3H-labeled L-Met and L-2-hydroxy-4-methylthiobutoanic acid (MHA-FA) was compared in germ-free and conventional broiler chickens to determine the effect of intestinal bacteria on the absorption of Met and MHA-FA. The two diets contained 0.236% of added Met or MHA-FA.

Enzymic release of reducing sugars from oat hulls by cellulase, as influenced by Aspergillus ferulic acid esterase and trichoderma xylanase.

Hydroxycinnamic acids, mainly ferulic and p-coumaric acids, are believed to be inhibitory to ruminal biodegradability of complex cell wall materials such as oat hulls. Previous studies have shown that a novel enzyme, Aspergillus ferulic acid esterase, and Trichoderma xylanase act synergistically to break the ester linkage between ferulic acid and the attached sugar of feruloyl polysaccharides, releasing ferulic acid from oat hulls. In this paper, we examined the enzymic release of reducing sugars from oat hulls by the actions of individual enzymes (Aspergillus ferulic acid esterase at 13 mU, 6.

Release of ferulic acid from oat hulls by Aspergillus ferulic acid esterase and trichoderma xylanase.

Oat hulls, an agricultural byproduct, contain a relatively high amount of ferulic acid (FA; 4-hydroxy-3-methoxycinnamic acid), which is believed to be inhibitory to oat hull biodegradability by rumen microorganisms. In this paper, Aspergillus ferulic acid esterase (FAE) was investigated for its ability to release FA from oat hulls. The objectives were to determine the effects of particle size of oat hulls (ground to pass through 1 mm and 250 microm screens and a 100 microm sieve) on release of FA by FAE both in the presence and in the absence of Trichoderma xylanase.