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Identification and characterization of an angiotensin-converting enzyme inhibitory peptide derived from bovine casein
38/38 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
9 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 38 checked references that resolve
resolves10.1016/j.cis.2010.11.001
Antihypertensive peptides: Production, bioavailability and incorporation into foods
resolves10.1016/j.peptides.2008.02.005
The antihypertensive effect of peptides: A novel alternative to drugs?
resolves10.1016/j.foodchem.2008.09.041
Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology
resolves10.1016/j.foodchem.2010.05.026
Production, analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein
resolves10.1016/j.jff.2014.01.025
Pilot-scale membrane fractionation of ACE inhibitory and antioxidative peptides from ultrasound pretreated milk protein concentrate hydrolysates
resolves10.1016/j.foodchem.2007.06.039
Antihypertensive effect of bioactive peptides produced by protease-facilitated lactic acid fermentation of milk
resolves10.1016/j.idairyj.2006.07.004
Purification of angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease-facilitated lactic fermentation
resolves10.1016/j.jff.2015.04.043
Purification and identification of novel peptides with inhibitory effect against angiotensin I-converting enzyme and optimization of process conditions in milk fermented with the yeast Kluyveromyces marxianus
resolves10.1016/j.idairyj.2010.01.007
Optimization of sour milk fermentation for the production of ACE-inhibitory peptides and purification of a novel peptide from whey protein hydrolysate
resolves10.3168/jds.S0022-0302(96)76487-1
Identification of an Antihypertensive Peptide from Casein Hydrolysate Produced by a Proteinase from Lactobacillus helveticus CP790
resolves10.1016/S0014-5793(02)03576-7
Angiotensin‐I‐converting enzyme inhibitory peptides from tryptic hydrolysate of bovine α<sub>S2</sub>‐casein
resolves10.1017/S0022029906002056
Yak Milk Casein as a Functional Ingredient: Preparation and Identification of Angiotensin-I-Converting Enzyme Inhibitory Peptides
resolves10.1016/j.peptides.2009.06.031
Stability to gastrointestinal enzymes and structure–activity relationship of β-casein-peptides with antihypertensive properties
resolves10.1016/j.foodchem.2013.06.089
Novel angiotensin I-converting enzyme inhibitory peptide derived from bovine casein
resolves10.1002/jsfa.5894
Angiotensin I‐converting enzyme inhibitory peptides derived from bovine casein and identified by <scp>MALDI‐TOF‐MS</scp>/<scp>MS</scp>
resolves10.1016/j.foodchem.2015.04.130
Peptide identification and angiotensin converting enzyme (ACE) inhibitory activity in prolyl endoproteinase digests of bovine αs-casein
resolves10.1016/j.jff.2013.07.013
Angiotensin-I converting enzyme (ACE) inhibitory tripeptides from rice protein hydrolysate: Purification and characterization
resolves10.1016/S0963-9969(01)00131-4
Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides
resolves10.1016/j.foodchem.2011.07.011
Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate
resolves10.1016/j.foodchem.2008.12.019
Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste
resolves10.1016/j.procbio.2012.08.019
Angiotensin I converting enzyme (ACE) inhibitory peptides from salmon byproduct protein hydrolysate by Alcalase hydrolysis
resolves10.1016/j.foodchem.2013.03.091
Nine novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) muscle protein hydrolysates and antihypertensive effect of the potent active peptide in spontaneously hypertensive rats
resolves10.1016/j.foodchem.2009.04.086
A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats
resolves10.1021/jf400865m
Glycinyl-Histidinyl-Serine (GHS), a Novel Rapeseed Protein-Derived Peptide Has Blood Pressure-Lowering Effect in Spontaneously Hypertensive Rats
resolves10.1016/j.idairyj.2011.02.004
Food-grade production of an antihypertensive casein hydrolysate and resistance of active peptides to drying and storage
resolves10.1631/jzus.B1300239
Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein
resolves10.1002/(SICI)1097-0282(1997)43:2<129::AID-BIP5>3.0.CO;2-X
Antihypertensive peptides derived from food proteins
resolves10.1016/j.idairyj.2004.04.007
Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion
resolves10.1111/j.1365-2621.2000.tb16049.x
Classification and Antihypertensive Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptides Derived from Food Proteins
resolves10.3168/jds.S0022-0302(05)73032-0
Angiotensin-Converting Enzyme Inhibitory Activity of Peptides Derived from Caprine Kefir
resolves10.1016/S0271-5317(04)00058-2
Angiotensin I–converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
resolves10.3168/jds.S0022-0302(94)77026-0
Antihypertensive Effect of the Peptides Derived from Casein by an Extracellular Proteinase from Lactobacillus helveticus CP790
resolves10.1002/mnfr.200900448
Changes in arterial blood pressure after single oral administration of milk‐casein‐derived peptides in spontaneously hypertensive rats
resolves10.1016/S0021-9258(19)86187-2
Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.
resolves10.1007/s00217-004-1004-4
Quantitative structure-activity relationship modelling of ACE-inhibitory peptides derived from milk proteins
The 9 references without a DOI — listed, not checked
no DOI — not checkedCross-talk of the renin-angiotensin and kallikrein-kinin systems
no DOI — not checkedInhibition of homogeneous angiotensin-converting enzyme of rabbit lung by synthetic venom peptides of Bothrops jararaca. BBA
no DOI — not checkedPepsin hydrolysis of casein for the preparation of ACE inhibitory peptides
no DOI — not checkedEffect of α −Casein hydrolysate on blood pressure in spontaneously hypertensive rats
no DOI — not checkedEffect of different drying methods on angiotensin converting enzyme inhibitory activity of peptides from bovine casein hydrolysate
no DOI — not checkedStudy on UF for the separation and purification of angiotensin converting enzyme inhibitory peptide
no DOI — not checkedQuantitative determination of ACE inhibitory peptides in casein hydrolyzate by RP-HPLC
no DOI — not checkedA peptide inhibitor of angiotensin I converting enzyme in the tryptic hydrolysate of casein
no DOI — not checkedAngiotensin I −Converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. isolation and bradykinin- potentiating activity on the uterus and the ileum of rats
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