Document Detail

Compositional analysis of proteins following hydrolysis by immobilized proteases.
MedLine Citation:
PMID:  6440887     Owner:  NLM     Status:  MEDLINE    
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.
F C Church; H E Swaisgood; G L Catignani
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of applied biochemistry     Volume:  6     ISSN:  0161-7354     ISO Abbreviation:  J. Appl. Biochem.     Publication Date:  1984 Aug 
Date Detail:
Created Date:  1985-03-14     Completed Date:  1985-03-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7908148     Medline TA:  J Appl Biochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  205-11     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis
Enzymes, Immobilized*
Hydrogen-Ion Concentration
Insulin / analysis
Lactoglobulins / analysis
Peptide Hydrolases*
Proteins / analysis*
Streptomyces griseus / enzymology
Reg. No./Substance:
0/Amino Acids; 0/Enzymes, Immobilized; 0/Lactoglobulins; 0/Proteins; 11061-68-0/Insulin; 643-79-8/o-Phthalaldehyde; EC 3.4.-/Peptide Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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