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  • Title: Compositional analysis of proteins following hydrolysis by immobilized proteases.
    Author: Church FC, Swaisgood HE, Catignani GL.
    Journal: J Appl Biochem; 1984 Aug; 6(4):205-11. PubMed ID: 6440887.
    Abstract:
    Pronase, proteinase K, carboxypeptidases A and B, aminopeptidase M, intestinal mucosa exopeptidases and prolidase, immobilized to derivatized controlled-pore glass beads, were used in a study of total enzymic hydrolysis of proteins. The combined use of immobilized enzymatic and acid hydrolysis, for assessment of protein quality, will give a more accurate chemical score than that afforded by acid hydrolysis alone. Amino acid analysis of enzymic hydrolysates of native protein substrates (beta-lactoglobulin and insulin) yielded 92% of the theoretical values and 103% of the values observed for standard acid hydrolysates. These results suggest that using a combination of immobilized proteases in concert gives essentially total hydrolysis of protein substrates in a time period (18-24 h) comparable to conventional acid hydrolysis methods.
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