Gelatin amino acids

Gelatine Amino acids (characteristic hyd roxy-proline) 9000-70-8 Soluble in hot water, sets to a gel on cooling... 

Where MW is the molecular weight (kD) and Wr is the rate of sub-unit weight (%) in raw materials. 50% amidation rates of aspartic and glutamic acids are supposed for peanut proteins, keratin, collagen, and gelatin. Amino acid ratios (mol/100 mol) -A-non-ionized polar (Asn, Cys, Gin, His, Ser, Thr, Tyr), -B- ionized polar (Arg, Asp, Glu, Lys) and -C- non-polar (Ala, He, Leu, Met, Phe, Pro, Trp, Val). S is the solubility of proteins according to Osborne classification I- in water, II- in diluted salt solutions, III-in diluted acidic or basic solutions, and IV- in ethanol (80%) solutions Miscellaneous associations. 

Gelatin can be a source of essential amino acids when used as a diet supplement and therapeutic agent. As such, it has been widely used in muscular disorders, peptic ulcers, and infant feeding, and to spur nail growth. Gelatin is not a complete protein for mammalian nutrition, however, since it is lacking in the essential amino acid tryptophan [73-22-3] and is deficient in sulfur-containing amino acids. 

Amino acids are the main components of proteins. Approximately twenty amino acids are common constituents of proteins (1) and are called protein amino acids, or primary protein amino acids because they are found in proteins as they emerge from the ribosome in the translation process of protein synthesis (2), or natural amino acids. In 1820 the simplest amino acid, glycine, was isolated from gelatin (3) the most recendy isolated, of nutritional importance, is L-threonine which was found (4) in 1935 to be a growth factor of rats. The history of the discoveries of the amino acids has been reviewed... 

It is in this way that most of what we call the natural amino acids have been discovered. Proteins from many sources—egg yolk, milk, animal tissues, plant seeds, gelatin, etc.—have been studied to learn what amino acids compose them. In this way about thirty of the natural amino acids have been identified. 

In an attempt to design the p-turn-peptide-mimics, aspartic acid (an amino acid also known as aspartate) and lysine (an amino acid especially found in gelatin and casein) were attached to each amine group of 1,3-diaminoada-mantane in the form of amide bonds. The term p-turn refers to a peptide chain that forms a tight loop such that the carbonyl oxygen of one residue is hydrogen... 

The property of thermal, reversible gelation is obtained by the addition of water-soluble proteins and protein degradation products to an aqueous solution of poly (vinyl alcohol) 2). Protein products such as albumin, gelatin, glue, a-amino acids, and their condensation products—diketopiperazines—may be used. A typical formulation for the preparation of a thermally reversible gel is ... 

Animal glue is a complex colloidal mixture of proteins. The related gelatins are also complex heterogeneous mixtures of proteins. They are strongly hydrophilic and rich in the amino acids glycine, proline, lysine, hydroxyproline and hydroxylysine. Casein is a phosphoprotein obtained from the milk of mammals. 

The number of different amino acids actually found in proteins is greater than the 20 in the DNA code. This is because some of them are produced by posttranslational modification. Hydroxyproline, for example, is not coded in DNA. Proline is inserted in the peptide chain and the hydroxy group is later added to the peptidically liked proline to form hydroxyproline. Although hydroxyproline is found in some proteins that are known to be haze active, such as gelatin, polyhydroxyproline (the synthetic homopolymer of hydroxyproline) forms no haze with... 

Glycine A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter. [NIH]... 

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