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Spectrophotometric Assay Using o-Phthaldialdehyde for Determination of Proteolysis in Milk and Isolated Milk Proteins

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Church, Frank C., Swaisgood, Harold E., Porter, David H., Catignani, George L.·1983·Journal of Dairy Science
DOI 10.3168/jds.s0022-0302(83)81926-2
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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.Moreover, the absorptivity of the adduct with both a-and e-amino groups of proteins is also similar and unaffected by local environment when proteins are denatured in sodium dodecyl sulfate.Thus, background is constant for a particular sample, and a-amino groups released by proteolysis can be quantitated accurately.Inclusion of sodium dodecyl sulfate in the assay provides a convenient way to terminate proteolysis and to insure full exposure and complete reaction of amino groups.Because all hydrolytic products are assayed, the method is more accurate than procedures that depend upon properties of aromatic residues (Hull and Lowry methods).Furthermore, the o-phthaldialdehyde spectrophotometric assay is more rapid and convenient than methods using ninhydrin, 2,4,6-trinitro-

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Research works printed but not linked: 36

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Cited by

Metadata

Authors
Church, F. C., Swaisgood, H. E., Porter, D. H., & Catignani, G. L.
Venue
Journal of Dairy Science
Publisher
American Dairy Science Association
Published
1983-06
Volume
66
Issue
6
Pages
1219-1227
ISSN
0022-0302 (ISSN-L)
DOI
10.3168/jds.s0022-0302(83)81926-2
OpenAlex
W1975630793
Cited by
1,547
References
0
FWCI
11.24
Type
journal article
Language
en
Open access
bronze
Licence

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