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LC-MS/MS Quantification of Bioactive Angiotensin I-Converting Enzyme Inhibitory Peptides in Rye Malt Sourdoughs

Hu, Ying, Stromeck, Achim, Loponen, Jussi, Lopes-Lutz, Daise, Schieber, Andreas, Gänzle, Michael G.
Journal of agricultural and food chemistry 2011 v.59 no.22 pp. 11983-11989
Cucurbita, Lactobacillus reuteri, barley, bioactive properties, bioinformatics, gluten, inhibitory concentration 50, malt, mass spectrometry, peptidyl-dipeptidase A, prolamins, proteinases, rye, sourdough, tripeptides, wheat
This study quantified antiotensin I-converting enzyme (ACE) inhibitory peptides in rye malt sourdoughs supplemented with gluten proteins and fermented with six strains of Lactobacillus spp. Bioinformatic analysis of prolamins from barley, rye, and wheat demonstrated that the ACE inhibitory peptides LQP, LLP, VPP, and IPP are frequently encrypted in their primary sequence. These tripeptides were quantified by liquid chromatography-tandem mass spectrometry. Tripeptide levels in sourdoughs were generally higher as compared to the chemically acidified controls. Sourdoughs fermented with different strains showed different concentrations of LQP and LLP. These differences corresponded to strain-specific differences in PepO and PepN activities. The highest levels of peptides VPP, IPP, LQP, and LLP, 0.23, 0.71, 1.09, and 0.09 mmol (kg DM)-1, respectively, were observed in rye malt: gluten sourdoughs fermented with Lactobacillus reuteri TMW 1.106 and added protease. These concentrations were 6-7 times higher as compared to sourdough without fungal protease and exceed the IC50 by 100-1000-fold.