Type

Journal Article

Authors

R P Ross
G F Fitzgerald
C Hill
O O'Sullivan
H Slattery
C Stanton
M Hayes

Subjects

Microbiology

Topics
binding sites chemical synthesis peptides molecular sequence data chromatography high pressure liquid amino acid sequence mass spectrometry peptidyl dipeptidase a models molecular caseins filtration lactobacillus metabolism inhibitory concentration 50 pharmacology isolation purification animals fermentation angiotensin converting enzyme inhibitors cattle chemistry captopril

Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors. (2007)

Abstract This work evaluated the angiotensin-converting-enzyme (ACE)-inhibitory activities of a bovine sodium caseinate fermentate generated using the proteolytic capabilities of the porcine small intestinal isolate Lactobacillus animalis DPC6134 (NCIMB deposit 41355). The crude 10-kDa L. animalis DPC6134 fermentate exhibited ACE-inhibitory activity of 85.51% (+/-15%) and had a 50% inhibitory concentration (IC50) of 0.8 mg protein/ml compared to captopril, which had an IC50 value of 0.005 mg/ml. Fractionation of the crude L. animalis DPC6134 fermentate by membrane filtration and reversed-phase high-performance liquid chromatography (HPLC) generated three bioactive fractions from a total of 72 fractions. Fractions 10, 19, and 43 displayed ACE-inhibitory activity percentages of 67.53 (+/-15), 83.71 (+/-19), and 42.36 (+/-11), respectively, where ACE inhibition was determined with 80 microl of the fractions with protein concentrations of 0.5 mg/ml. HPLC and mass spectrometry analysis identified 25 distinct peptide sequences derived from alpha-, beta-, and kappa-caseins. In silico predictions, based on the C-terminal tetrapeptide sequences, suggested that peptide NIPPLTQTPVVVPPFIQ, corresponding to beta-casein f(73-89); peptide IGSENSEKTTMP, corresponding to alpha(s1)-casein f(201212); peptide SQSKVLPVPQ, corresponding to beta-casein f(166-175); peptide MPFPKYPVEP, corresponding to beta-casein f(124133); and peptide EPVLGPVRGPFP, corresponding to beta-casein f(210-221), contained ACE-inhibitory activities. These peptides were chosen for chemical synthesis to confirm the ACE-inhibitory activity of the fractions. Chemically synthesized peptides displayed IC50 values in the range of 92 microM to 790 microM. Additionally, a simulated gastrointestinal digestion confirmed that the ACE-inhibitory 10-kDa L. animalis DPC6134 fermentation was resistant to a cocktail of digestive enzymes found in the gastrointestinal tract.
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Full list of authors on original publication

R P Ross, G F Fitzgerald, C Hill, O O'Sullivan, H Slattery, C Stanton, M Hayes

Experts in our system

1
R Paul Ross
Teagasc
Total Publications: 441
 
2
Gerald F Fitzgerald
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Total Publications: 207
 
3
Colin Hill
University College Cork
Total Publications: 351
 
4
Orla O'Sullivan
Teagasc
Total Publications: 92
 
5
Catherine Stanton
Teagasc
Total Publications: 261
 
6
Maria Hayes
Teagasc
Total Publications: 34