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Hydrosylates for Recovery
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Hydrosylates for Recovery
Tailored whey protein molecular weight (MW) peptide hydrolysates (peptide-based protein) have been prescribed by the medical community for many years to promote more effective protein absorption and assimilation. Whey hydrolysates promote optimal nitrogen retention in those recovering from abdominal surgery, short bowel, and other patients with compromised intestinal dysfunction. For a number of reasons I suspect high quality whey hydrolysate would be just as effective for hepatic regulation.
Whey proteins are absorbed in the human GI tract differently than other proteins. When clinical diets were first formulated it was generally believed that dietary protein required complete hydrolysis to free amino acids before any absorption in the upper jejunum took place. However, reports have already concluded that intact peptide absorption occurs in the small intestine of adult animals. Dietary proteins are mainly degraded by luminal enzymes in the GI tract. But some, like those found in whey protein, escape the hydrolytic process and reach the intestinal mucosa in peptide form and are absorbed intact. A full spectrum of whey hydrolysates are shown to be absorbed faster (20-40min) and in greater amounts than other quality proteins.
Whey protein’s major components, B-lactoglobulin and a-lactalbumin, have been found in an intact, antigenic form in the lumen and have been shown to be transported intact across the small intestinal mucosa. These proteins found in whey appear to have very different gastrojejunal kinetics to casein (the other major milk protein). B-lactoglobulin transits more rapidly than casein to the upper jejunum and remains soluble in the stomach and empties more rapidly while casein clots, forms precipitate and empties more slowly. B-lactoglobulin is absorbed as intact peptides, unlike casein, which must be first exposed to gastric hydrolysis. The immunoglobulins (antigens) preserved in quality whey protein formulations are shown to be absorbed intact in the upper jejunum (this is a pretty amazing thing).Whey protein peptides appear to be transferred by macromolecular pathways, and pass through the epithelium by paracellular (between epithelial cells) or transcellular (through the cell) mechanisms, utilizing both receptor-meditated and non-receptor meditated (epithelial M cell) transport.
Whey protein provides a spectrum of lower MW peptides (500-15 000 D) combined with medium to high MW peptides (14 000 -160 000+ D). This is important as this peptide profile is shown to provide superior steady-state nitrogen absorption and immune-enhancing qualities and it is more effective than whole protein sources or free form amino acid mixtures for those with compromised digestion capabilities.
If a protein possesses these very favorable absorption/assimilation capabilities then hepatic burden of urea metabolism is greatly reduced. Nitrogenous wastes like ammonia are excreted by the kidneys, the liver has only moderate urea regulation abilities. However the liver does determine the extent of urea formation and degradation from food sources. Therefore based on the above facts I can only suggest whey hydrolysates would be a far better protein choice in this instance.
Whey proteins are absorbed in the human GI tract differently than other proteins. When clinical diets were first formulated it was generally believed that dietary protein required complete hydrolysis to free amino acids before any absorption in the upper jejunum took place. However, reports have already concluded that intact peptide absorption occurs in the small intestine of adult animals. Dietary proteins are mainly degraded by luminal enzymes in the GI tract. But some, like those found in whey protein, escape the hydrolytic process and reach the intestinal mucosa in peptide form and are absorbed intact. A full spectrum of whey hydrolysates are shown to be absorbed faster (20-40min) and in greater amounts than other quality proteins.
Whey protein’s major components, B-lactoglobulin and a-lactalbumin, have been found in an intact, antigenic form in the lumen and have been shown to be transported intact across the small intestinal mucosa. These proteins found in whey appear to have very different gastrojejunal kinetics to casein (the other major milk protein). B-lactoglobulin transits more rapidly than casein to the upper jejunum and remains soluble in the stomach and empties more rapidly while casein clots, forms precipitate and empties more slowly. B-lactoglobulin is absorbed as intact peptides, unlike casein, which must be first exposed to gastric hydrolysis. The immunoglobulins (antigens) preserved in quality whey protein formulations are shown to be absorbed intact in the upper jejunum (this is a pretty amazing thing).Whey protein peptides appear to be transferred by macromolecular pathways, and pass through the epithelium by paracellular (between epithelial cells) or transcellular (through the cell) mechanisms, utilizing both receptor-meditated and non-receptor meditated (epithelial M cell) transport.
Whey protein provides a spectrum of lower MW peptides (500-15 000 D) combined with medium to high MW peptides (14 000 -160 000+ D). This is important as this peptide profile is shown to provide superior steady-state nitrogen absorption and immune-enhancing qualities and it is more effective than whole protein sources or free form amino acid mixtures for those with compromised digestion capabilities.
If a protein possesses these very favorable absorption/assimilation capabilities then hepatic burden of urea metabolism is greatly reduced. Nitrogenous wastes like ammonia are excreted by the kidneys, the liver has only moderate urea regulation abilities. However the liver does determine the extent of urea formation and degradation from food sources. Therefore based on the above facts I can only suggest whey hydrolysates would be a far better protein choice in this instance.
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