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Extra info for Amino Acids in Animal Nutrition
Colorimetric assays of tryptophan have been mentioned above. Available/reactive lysine Lysine in protein is highly susceptible to damage through heat treatment as it possesses a reactive ⑀-amino group, especially if reducing sugars are present. , 1994) are no longer available for animal or human protein synthesis. In 1960 Carpenter introduced an in vitro test for available, better reactive lysine, in which the protein was reacted with fluoro-2,4dinitrobenzene (FDNB) and the resulting 28 J. Fontaine coloured dinitrophenyl (DNP)-lysine was determined photometrically following hydrolysis.
1996) Selective biosensing of L-lysine by a low-temperature flow-injection technique using an immobilized lysine oxidase reactor. Analytical Sciences 12, 87–90. A. M. (1994) Applications of amino acid derivatization with 6-aminoquinolylN-hydroxysuccinimidyl carbamate. Analysis of feed grains, intravenous solutions and glycoproteins. Journal of Chromatography A 661, 25–34. A. P. (1993) Synthesis of a fluorescent derivatizing reagent, 6-aminoquinolyl-Nhydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino-acids via high-performance liquid chromatography.
A fluorimetric assay of lysine in feed hydrolysate following reaction with L-lysine oxidase was described by Hikuma et al. (1991) which showed a high degree of concordance with IEC for compound feeds, fish meal and soy. Ninhydrin-ferric reagent was used by Hsieh et al. (1995) for the determination of lysine in culture broth. Colorimetric assays of tryptophan have been mentioned above. Available/reactive lysine Lysine in protein is highly susceptible to damage through heat treatment as it possesses a reactive ⑀-amino group, especially if reducing sugars are present.
Amino Acids in Animal Nutrition by D_Mello