Partially Hydrolyzed Protein

Elemental or peptide-based formulations have partially hydrolyzed protein or fat components. Peptide-based formulations replace some of the protein with dipeptides and tripeptides, thereby optimizing absorption in patients with impaired digestive or absorptive capacity. 

Mietsch, F., Feher, J., and Halasz, A. 1989. Investigation of functional properties of partially hydrolyzed proteins. Nahrung 33, 9-15. 

Note Depending on the protein source and the degree of hydrolysis, Partially Hydrolyzed Proteins may present an allergenic risk to sensitized individuals. 

More detailed discussion of food polymers and their functionality in food is now difficult because of the lack of the information available on thermodynamic properties of biopolymer mixtures. So far, the phase behaviour of many important model systems remains unstudied. This particularly relates to systems containing (i) more than two biopolymers, (ii) mixtures containing denatured proteins, (iii) partially hydrolyzed proteins, (iv) soluble electrostatic protein-polysaccharide complexes and conjugates, (v) enzymes (proteolytic and amylolytic) and their partition coefficient between the phases of protein-polysaccharide mixtures, (vi) phase behaviour of hydrolytic enzyme-exopolysaccharide mixtures, exopolysaccharide-cell wall polysaccharide mixtures and exopolysaccharide-exudative polysaccharide mixtures, (vii) biopolymer solutes in the gel networks of one or several of them, (viii) enzymes in the gel of their substrates, (ix) virus-exopolysaccharide, virus-mucopolysaccharides and virus-exudative gum mixtures, and so on. 

Acylated Polypeptides (From partially hydrolyzed protein from scrap leather and other waste protein.) Used in hair preparations and shampoos, alkaline cleaning preparations, wax strippers. Good detergency and resistance to hard water. 

Schmelzle, H., Wirth, S., Skopnik, H., Radke, M., Knol, J., Bockler, H. M., Fusch, C. (2003). Randomized Double-Blind Study of the Nutritional Efficacy and Bifidogenicity of a New Infant Formula Containing Partially Hydrolyzed Protein, a High P-Palmitic Acid Level, and Nondigestible Ohgosaccharides. J Pediatr Gastroenterol Nutr, 36(3), 343-351. 

Thin-layer chromatography (TLC) and the more modem technique—high-performance thin-layer chromatography (HPTLC)— have numerous applications in proteins chemistry. These techniques are used for the quantitative determinations of peptides (nanograms), identification of peptides in partially hydrolyzed proteins, correlation of chromatographic properties for peptides and their constituent amino acids, as well as identification and characterization of proteins present in small quantities. 

Note also that ammonium sulfate is absent from the recommended binding buffer formulations despite its general popularity in the field. Ammonium ions become fully titrated at alkaline pH and convert to ammonia gas. Buffer pH may become unstable as a result and causticity of the free ammonia may partially hydrolyze the proteins in a sample, creating a source of assay variability.617 18 At small buffer volumes used for analytical applications, liberated ammonia gas may not be a significant health hazard, but precautions may still be necessary to meet regulations. For all these reasons, ammonium salts are best avoided at alkaline pH. 

As already known, amino acids are the building units of peptides and proteins and they play an important plastic, energetic, and regulatory role in all living organisms. Almost all foods contain amino acids, either in the bound (partially hydrolyzed or intact proteins) or in the free form. High amounts of free amino acids can be found in some fermented foodstuffs as a consequence of proteolytic processes. 

Considerable effort has been devoted to the improvement of functional properties of fish protein concentrate. Spinelli et al. (44) conducted a study to determine the feasibility of modifying myofibrillar fish proteins by partially hydrolyzing them... 

The kinetics of the lytic effect displayed by the complexes of immobilized heparin with thrombin and fibrinogen, in distinction from those with plasmin, are described by their saturation curves. The observed slowing down of the dissolution of unstabilized fibrin is probably due to the inhibiton of the lytic activity of the complexes by the soluble products of the reaction. In fact, as it was shown in Ref. 106, further addition of immobilized heparin-protein complex to partially hydrolyzed fibrin results in a complete recovery of the dissolution rate. 

The overwhelming majority of foods contain amino acids, either in the free form (e.g., fruit juice) or in the form of protein (partially hydrolyzed or intact). Proteins are polymers, and their monomeric units are amino acids. Predominantly, proteins are comprised of 20 amino acids (see Fig. 1). In addition, some structural proteins contain large amounts of hydroxyproline (e.g., collagen). Far less abundant is the amino acid hydroxy lysine. The principal sources of dietary amino acids for humans are proteins, which are enzymatically digested to liberate their constituent amino acids. 

After the sequence of the individual chains has been determined, a sample of the protein is partially hydrolyzed without cleavage of the disulfide bonds, and the fragments containing the intact disulfide bonds are sequenced. 

Plastein Formation. Plastein formation is another example of using proteases to modify high-protein food systems to drastically change the properties of that system (II). In the plastein reaction a protease such as papain is used to partially hydrolyze the proteins to about a 10,000-20,000-dalton size at a pH near neutrality. After concentrating the hydrolyzate to 35% (based on protein) and a change in pH, the same protease or a different one is used to catalyze the resynthesis of a few peptide bonds. This may result in a decrease in the solubility of the protein. 

Naturally the implication arose that there should be a high incidence of common peptides in the partial hydrolyzates of each of the serum proteins. This, of course, is the same implication that arose in Block s mind (3). Since 1956 this laboratory has been busy trying to isolate common peptides from each of the serum proteins as obtained from electrophoresis on starch slabs. In order to be able to prepare each of the protein hydrolyzates simultaneously we examined nonenzy-matic procedures and devised the dilute acid partial hydrolyzate method which has recently been described in detail (33, 34). In this method aspartic acid is preferentially eliminated from the peptide chain, the re-... 

Enzyme-Hydrolyzed (Source) Protein Partially Hydrolyzed (Source) Protein (Source) Peptone Enzyme-Modified (Source) Protein Partial Enzymatic Digest of (Source) Protein Partial Acid Digest of (Source) Protein... 

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