Abstract

A method is described for the comprehensive characterization of protein hydrolysates for enteral nutrition. It includes (1) gel filtration on a 0.9×250 cm column of Sephadex G-25F eluted with 5% acetic acid, to prepare pools; (2) amino acid analysis with and without acid hydrolysis to determine the amounts of peptide bound and free amino acids; (3) reaction with TNBS to determine the amount of NH 2 -terminal groups; and (4) calculation of number-average peptide size of pools from TNBS and amino acid data. The preparation of three hydrolysates of casein with pancreatic enzymes on the industrial scale (5000 L) is described

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