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Milk-derived angiotensin-I-converting enzymeinhibitory peptides generated by Lactobacillus delbrueckii subsp. lactis CRL 581

100%
Villegas J. M., Picariello G., Mamone G., Espeche Turbay M. B., Savoy de Giori G., Hebert E. M.
Peptidomics
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2014
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vol. 1
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issue 1
EN
Several strains of Lactobacillus helveticus and Lactobacillus delbrueckii subsp. lactis were evaluated for their ability to release angiotensin-I-converting enzyme (ACE) inhibitory peptides from α-casein (α-CN) and β-casein (β-CN). Casein peptides resulting from L. delbrueckii subsp. lactis CRL 581-mediated hydrolysis exhibited the highest ACE-inhibitory (ACEI) activities, with values of 53 and 40% for α-CN and β-CN, respectively. The casein hydrolysates were fractionated by reversedphase high pressure liquid chromatography and some of the active peptides were identified by mass spectrometry. The fraction with the highest ACEI activity arose from β-CN and contained a mixture of the β-CN f194-206 (QEPVLGPVRGPFP) and f198-206 (LGPVRGPFP) peptides. Furthermore, the ACEI tripeptide IPP was identified in all β-CN hydrolysates; L. delbrueckii subsp. lactis CRL 581 produced the highest amount of this peptide. The bioactive peptides released by CRL 581 strain may be used in the formulation of functional foods and nutraceuticals, representing a healthier and natural alternative for regulating blood pressure.
2
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Co-expression and characterization of enterocin CRL35 and its mutant in Escherichia coli Rosetta

84%
Masías E., Picariello G., Acuña L., Chalón M., Sesma F., Morero R., Saavedra L., Minahk C.
Peptidomics
|
2014
|
vol. 1
|
issue 1
EN
Even though many sequences and structures of bacteriocins from lactic acid bacteria have been fully characterized so far, little information is currently available about bacteriocins heterologously produced by Escherichia coli. For this purpose, the structural gene of enterocin CRL35, munA, was PCR-amplified using specific primers and cloned downstream of PelB sequence in the pET22b (+) expression vector. E. coli Rosetta (DE3) pLysS was chosen as the host for production and enterocin was purified by an easy two-step protocol. The bacteriocin was correctly expressed with the expected intramolecular disulfide bond. Nevertheless, it was found that a variant of the enterocin, differing by 12 Da from the native polypeptide, was co-expressed by E. coli Rosetta in comparable amount. Indeed, the mutant bacteriocin contained two amino acid substitutions that were characterized by matrix assisted laser desorption ionization-time of flight (MALDI-TOF) and HPLCelectrospray (ESI)-Q-TOF tandem mass spectrometry (MS/ MS) sequencing. This is the first report regarding the production of mutants of pediocin-like bacteriocins in the E. coli expression system.
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