Amino Acid Analysis

Amino acid analysis is used to determine the amino acid content of amino acid–, peptide- and protein-containing samples. With minor exceptions, proteins are long linear polymers of amino acids connected to each other via peptide bonds. The first step of amino acid analysis involves hydrolyzing these peptide bonds. The liberated amino acids are then separated, detected, and quantified. The method was first developed by Moore, Stein and coworkers in the 1950s using HCl acid hydrolysis, and, despite considerable effort by many workers, the basic methodology remains relatively unchanged. This unit provides an overview and strategic planning for amino acid analysis, discussing a range of methodologies and issues. In addition, several common methods used for analysis of l-amino acids are described in detail, including: HCl acid hydrolysis, performic acid oxidation for methionine and cysteine analysis, base hydrolysis for tryptophan analysis, analysis of free amino acids, and analysis of reactive lysine

Felinine stability in the presence of selected urine compounds

The stability of felinine, an amino acid present in feline urine, was investigated. Synthetic felinine was unstable in the urine of a selection of mammals. Felinine was found to stable in feline urine in which urea had been degraded. Synthetic felinine was found to react specifically with urea and did not react with urea analogues such as biuret or thiourea or other nucleophilic compounds such as ammonia which is more nucleophilic or acetamide and water which are less nucleophilic than urea. The reaction of urea and felinine was independent of pH over the range of 3¿10. Urea did not react with N-acetyl-felinine suggesting a felinine N-terminal interaction with urea. Mass spectral analysis of the reaction products showed the presence of carbamylated felinine and fragmentation ions derived from carbamyl-felinine. The physiological relevance of felinine carbamylation is yet to be determined

True ileal amino acid digestibility of goat and cow milk infant formulas

Goat milk is used as an alternative to cow milk for the production of infant formulas. However, little is known about the protein quality and, specifically, about the digestible AA pattern of goat milk formulas compared with their cow milk counterparts. In this study, the true ileal AA digestibility of a goat milk infant formula was compared with a premium cow milk infant formula. The 3-wk-old piglet was used as a model for the 3-mo-old infant. Both milk formulas were prepared as described by the manufacturer, with titanium dioxide added as an indigestible marker. The formulas were fed to the piglets over a 2-wk trial period. Digesta from the terminal ileum were collected post euthanasia and analyzed for AA content, along with samples of the formulas. True AA digestibility was determined after correcting for endogenous AA loss at the terminal ileum of pigs fed an enzyme-hydrolyzed casein-based diet, followed by ultrafiltration (5,000 Da) of the digesta. Total urine and feces collection was also undertaken to determine the nitrogen retention from the diets. The true ileal AA digestibility was similar between the goat and cow milk infant formulas for all AA except Gly and Trp. There was no significant difference in the nitrogen retention of piglets fed the two different formulas. The goat milk infant formula and the premium cow milk infant formula were similar in terms of protein qualit