1985
DOI: 10.1271/bbb1961.49.2587
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Studies of bitter peptides from casein hydrolyzate. Part XI. Bitter taste of synthetic C-terminal tetradecapeptide of bovine .BETA.-casein, H-Pro196-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val209-OH, and its related peptides.

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Cited by 22 publications
(3 citation statements)
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“…In comparison, the identified peptide β-CN(198–206), which is a segment of β-CN(193–209), showed a 6-fold higher threshold concentration of 1.18 mmol/L. Literature studies on segments within the sequence β-CN(193–209) revealed that the fragment aa(202–209) is required for intense bitter taste; for example, the thresholds reported for the peptides aa(196–209), aa(200–209), and aa(202–209) were found to be below 0.02 mmol/L .…”
Section: Resultsmentioning
confidence: 93%
See 1 more Smart Citation
“…In comparison, the identified peptide β-CN(198–206), which is a segment of β-CN(193–209), showed a 6-fold higher threshold concentration of 1.18 mmol/L. Literature studies on segments within the sequence β-CN(193–209) revealed that the fragment aa(202–209) is required for intense bitter taste; for example, the thresholds reported for the peptides aa(196–209), aa(200–209), and aa(202–209) were found to be below 0.02 mmol/L .…”
Section: Resultsmentioning
confidence: 93%
“…The threshold of the "bitter flavor defect" peptide β- was found to be 0.18 mmol/L, which is well in agreement with previously reported data (41,42). In comparison, the identified peptide β- , which is a segment of β- , showed a 6-fold higher threshold concentration of 1.18 mmol/ L.Literaturestudiesonsegmentswithinthesequenceβ-CN(193-209) revealed that the fragment aa(202-209) is required for intense bitter taste; for example, the thresholds reported for the peptides aa (196)(197)(198)(199)(200)(201)(202)(203)(204)(205)(206)(207)(208)(209), aa(200-209), and aa(202-209) were found to be below 0.02 mmol/L (43).…”
Section: Resultsmentioning
confidence: 99%
“…The milk peptide database generated in the present study was applied to identify bioactive peptide sequences already present in milk. Out of the 22 peptides, for which bioactivity has been reported before, eight peptides have an inhibitory effect on the angiotensin-converting enzyme or have an antihypertensive effect. Eight peptides cause a bitter taste. An immunomodulating effect has been reported for three peptides, , antimicrobial properties for three peptides, and an antioxidative effect for two peptides. , Furthermore, a peptide which inhibits prolyl endopeptidases linked to amnesia and one peptide interacting with calmodulin were found . Casecidin 17 (β-casein 193–209 ) shows plurifunctional properties including immunomodulation, bitter taste, ACE-inhibition, and antimicrobial activity. ,− , Isracidin (α S1 -casein 1–23 ) displays antimicrobial and immunomodulating properties, and the fragment FALPQYLK (α S2 -casein 174–181 ) shows antioxidant and ACE-inhibitory effects. , α S1 -Casein 23–34 is described as bitter and ACE-inhibitory. ,,, However, it can be assumed that the physiological activity of the majority of peptides has not been tested so far, so that the description of the endogenous milk peptidome may help to identify novel bioactive peptides, for example, by the generation of peptide libraries, which can be subjected to screening assays.…”
Section: Discussionmentioning
confidence: 97%