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Spectrophotometric Assay Using o-Phthaldialdehyde for Determination of Proteolysis in Milk and Isolated Milk Proteins
Journal of Dairy Science · 1983 · Vol. 66(6) · pp. 1219–1227
Frank Church✉(North Carolina State University)Harold E. Swaisgood(North Carolina State University)David H. Porter(North Carolina State University)George L. Catignani(North Carolina State University)
Abstract
A rapid, sensitive, and convenient spectrophotometric assay was developed and characterized for measurement of proteolysis of milk proteins in buffered solutions or in milk. a-Amino groups released by hydrolysis react with o-phthaldialdehyde and /3-mercaptoethanol to form an adduct that absorbs strongly at 340 nm. The absorptivity (e = 6000 M -1 cm -1) is similar for all oe-amino groups.
Protein Hydrolysis and Bioactive PeptidesMeat and Animal Product QualityProteins in Food SystemsProteolysisChemistryChromatographyNinhydrinAdductSodium dodecyl sulfateHydrolysisMolar absorptivitySodiumAmino acid
Funding
- U.S. Department of Agriculture
Citations
1,507
FWCI
1.96
field-weighted impact
References
33
Percentile
86%
vs. same field & year
Citations per year
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References
A MODIFIED NINHYDRIN REAGENT FOR THE PHOTOMETRIC DETERMINATION OF AMINO ACIDS AND RELATED COMPOUNDS
Journal of Biological Chemistry · 1954 · 3,043 citations
ON TYROSINE AND TRYPTOPHANE DETERMINATIONS IN PROTEINS
Journal of Biological Chemistry · 1927 · 2,916 citations
Assay of proteins in the presence of interfering materials
Analytical Biochemistry · 1976 · 3,203 citations
Fluorescence reaction for amino acids
Analytical Chemistry · 1971 · 1,347 citations
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