IRIS publication 243941792
Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors
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TY - JOUR - Hayes, M,Stanton, C,Slattery, H,O'Sullivan, O,Hill, C,Fitzgerald, GF,Ross, RP - 2007 - July - Applied and Environmental Microbiology - Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors - Validated - WOS: 105 () - LACTIC-ACID BACTERIA BIOACTIVE PEPTIDES BETA-CASEIN LACTOCOCCUS-LACTIS BOUND PROTEINASE MILK-PROTEINS HYDROLYSATE BINDING RECONSTRUCTION IDENTIFICATION - 73 - 4658 - 4667 - 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 mu l 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 NIPPLTQTPWVPPFIQ, 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 R-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 mu M to 790 mu M. 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. - 10.1128/AEM.00096-07 DA - 2007/07 ER -
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@article{V243941792, = {Hayes, M and Stanton, C and Slattery, H and O'Sullivan, O and Hill, C and Fitzgerald, GF and Ross, RP }, = {2007}, = {July}, = {Applied and Environmental Microbiology}, = {Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors}, = {Validated}, = {WOS: 105 ()}, = {LACTIC-ACID BACTERIA BIOACTIVE PEPTIDES BETA-CASEIN LACTOCOCCUS-LACTIS BOUND PROTEINASE MILK-PROTEINS HYDROLYSATE BINDING RECONSTRUCTION IDENTIFICATION}, = {73}, pages = {4658--4667}, = {{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 mu l 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 NIPPLTQTPWVPPFIQ, 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 R-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 mu M to 790 mu M. 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.}}, = {10.1128/AEM.00096-07}, source = {IRIS} }
Data as stored in IRIS
AUTHORS | Hayes, M,Stanton, C,Slattery, H,O'Sullivan, O,Hill, C,Fitzgerald, GF,Ross, RP | ||
YEAR | 2007 | ||
MONTH | July | ||
JOURNAL_CODE | Applied and Environmental Microbiology | ||
TITLE | Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors | ||
STATUS | Validated | ||
TIMES_CITED | WOS: 105 () | ||
SEARCH_KEYWORD | LACTIC-ACID BACTERIA BIOACTIVE PEPTIDES BETA-CASEIN LACTOCOCCUS-LACTIS BOUND PROTEINASE MILK-PROTEINS HYDROLYSATE BINDING RECONSTRUCTION IDENTIFICATION | ||
VOLUME | 73 | ||
ISSUE | |||
START_PAGE | 4658 | ||
END_PAGE | 4667 | ||
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 mu l 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 NIPPLTQTPWVPPFIQ, 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 R-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 mu M to 790 mu M. 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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DOI_LINK | 10.1128/AEM.00096-07 | ||
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