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Literature summary for 3.4.21.7 extracted from

  • Dalsgaard, T.K.; Heegaard, C.W.; Larsen, L.B.
    Plasmin digestion of photooxidized milk proteins (2008), J. Dairy Sci., 91, 2175-2183.
    View publication on PubMed
Search for more literature for 3.4.21.7

Application

Application Comment Organism
nutrition hydrolysis of milk proteins alphaS-casein, beta-casein, kappa-casein, alpha-lactalbumin, beta-lactoglobulin, and lactoferrin is highly dependent on photooxidation state of substrate. Changes in the formation of potential angiotensin I-converting enzyme-inhibitory peptides as well as peptides proposed to have anti-bactericidal activities are observed after oxidation of substrates before plasmin hydrolysis Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-lactalbumin + H2O hydrolysis is highly dependent on photooxidation state of substrate Bos taurus ?
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 ?
alphaS-casein + H2O hydrolysis is highly dependent on photooxidation state of substrate Bos taurus ?
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 ?
beta-casein + H2O hydrolysis is highly dependent on photooxidation state of substrate Bos taurus ?
-
 ?
beta-lactoglobulin + H2O hydrolysis is highly dependent on photooxidation state of substrate Bos taurus ?
-
 ?
kappa-casein + H2O hydrolysis is highly dependent on photooxidation state of substrate Bos taurus ?
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 ?
lactoferrin + H2O hydrolysis is highly dependent on photooxidation state of substrate Bos taurus ?
-
 ?