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STUDIES CONCERNING THE DETERMINATION OF LYSINOALANINE IN FOOD PROTEINS
Author(s) -
RAYMOND MARVIN L.
Publication year - 1980
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1980.tb03869.x
Subject(s) - ninhydrin , chemistry , chromatography , sodium , hydrolysis , sodium citrate , amino acid , food science , biochemistry , organic chemistry , medicine , pathology
A study was made on the use of an amino acid analyzer for determining lysinoalanine (LAL) in food proteins. Protein bound lysinoalanine is liberated by acid hydrolysis, separated on a high pressure cation exchange column with a sodium citrate buffer (0.35N sodium; pH 5.30), and detected calorimetrically after reaction with ninhydrin. The procedure is sensitive to concentrations of 50 pg LAL/g sample and concentrations as low as 20 μg/g sample have been detected. Application to food products, problems encountered, and the use of two different column temperatures (52 and 65°C) for different products to achieve better separation are described.