Gelatin peptides

Kim, G. H., Jeon, Y. J., Byun, H. G., Lee, Y. S., and Kim, S. K. (1998). Effect of calcium compounds from oyster shell bound fish skin gelatine peptide in calcium deficient rats. J. Korean Fish. Soc. 31,149-159. 

Gelatin peptides have repeated unique Gly-Pro-Ala sequence in their structure, and it is presumed that the observed antioxidative properties of gelatin peptides can be associated with their unique amino acid compositions. 

In addition, gelatin peptides have shown to accelerate absorption of dietary calcium in animal models increasing calcium bioavailability (Kim et al., 1998). Jung et al. (2006) reported that fish bone peptides (FBP) could inhibit the formation of insoluble Ca salts in neutral pFI. During the experimental period, Ca retention was increased and loss of bone mineral was decreased by FBP II supplementation in ovariectomized rats. The levels of femoral total Ca, bone mineral density, and strength were also significantly increased by the FBP diet to levels similar to those of the casein phosphopeptide diet group. 

Our research group has reported in a series of papers that production of enzymes from PLLA degrading microorganisms was induced when some proteins such as silk fibroin, elastin, gelatin, peptides, and some amino acids were present in the cultivation medium [27, 44—46, 48]. For instance, a significant increase in the enzyme activity of Amycolatopsis strain HT-41 was detected when silk fibroin was added into the culture medium [44]. Moreover, various amino acids, peptides, and poly(L-amino acids) were used as enzyme inducers for the production of enzymes from T. albtm, L. waywandensis, and A. orientalis. Silk fibroin was found to be the best inducer for A. orientalis. On the other hand, the enzyme activities of L. waywandensis and T. album were stimulated by elastin but not by silk fibroin. Soluble culture substrates such as peptides and amino acids had lower induction activities in comparison to protein substrates (silk fibroin, elastin, collagen, and keratin) [48]. 

The fish collagen swells limited in water and produces a suspension, which stables in acid medium. The concentration of amino group according to formalin titration in the fish collagen was 1.1 mol/g. The fish collagen contains in 10% more amino group then the gelatin peptides. 

Amphoteric hydrophobic Blue dextran, collagen, gelatin, hydrophobic proteins Hydrophobic peptides Buffer or salt solution with organic solvent (e,g, 20% CH3CN in 0.1 M NaNOi) 35-45% CH3CN in 0.1% TFA... 

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 usual alkali employed is lime. The raw material for gelatine is tropocollagen, which is present in the original hides or bones. This protein consists of three polypeptide chains arranged in a triple helix. In contrast, gelatine consists of several free or interassociated chains, ranging in molecular weight from around ten thousand to several hundred thousand. On extraction, monomers (a-chains MW 100 000), dimers (P-chains) and trimers ( -chains) and some lower order peptides are released. 

Wang J, Sakai S, Deguchi Y, Bi D, Tabata Y, Morimoto K (2002) Aminated gelatin as a nasal absorption enhancer for peptide drugs evaluation of absorption enhancing effect and nasal mucosa perturbation in rats. J Pharm Pharmacol 54 181— 188. 

J. Wang, Y. Tabata, and K. Morimoto. Aminated gelatin microspheres as a nasal delivery system for peptide drugs Evaluation of in vitro release and in vivo insulin absorption in rats. J Control Release 113 31-37 (2006). 

Gelatin colloids consist of cross-Unked peptide chains obtained from collagen. They are employed for blood replacement, but not for hemodilution, in circulatory disturbances. 

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... 

A variation on the Thompson and Forward method was developed in which a HA peptide or peptide-like material (e.g., gelatin, gliadin, polyproline, or soluble polyvinylpyrrolidone) is added to a sample to induce haze in proportion to the amount of HA polyphenol it contains (Siebert et al., 1996a). This gives little response in beer, which contains very little HA polyphenol, and causes much larger haze increases in fruit juices and wine. 

Mendis, E., Rajapakse, N., and Kim, S. K. (2005). Antioxidant properties of a radicals scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. ]. Agric. Food Chem. 53, 581-587. 

Aleman, A., Gimenez, B., Perez-Santin, E., Gomez-Guillen, M. C., and Monter, P. (2011). Contribution of Leu and Hyp residues to antioxidant and ACE-inhibitory activities of peptide sequences isolated from squid gelatin hydrolysate. Food Chem. 125, 334-341. 

Zhao, Y., Li, B., Liu, Z., Dong, S., Zhao, X., and Zeng, M. (2007). Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate. Process Biochem. 42, 1586-1591. 

B. Peptides from fish skin collagen and gelatin 238... 

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