Insights Into the Complexity of Yeast Extract Peptides and Their Utilization by Streptococcus thermophilus

被引:24
作者
Proust, Lucas [1 ,2 ]
Sourabie, Alain [2 ]
Pedersen, Martin [3 ]
Besancon, Iris [2 ]
Haudebourg, Eloi [1 ]
Monnet, Veronique [1 ]
Juillard, Vincent [1 ]
机构
[1] Univ Paris Saclay, INRA, Micalis Inst, AgroParisTech, Jouy En Josas, France
[2] Lesaffre Grp, Procelys, Maisons Alfort, France
[3] Sacco Srl, Cadorago, Italy
关键词
Streptococcus thermophilus; yeast extract; peptidomics; oligopeptide; transport; OLIGOPEPTIDE TRANSPORT-SYSTEM; FREE AMINO-ACIDS; LACTOCOCCUS-LACTIS; SUBSTRATE-SPECIFICITY; PROTEOLYTIC SYSTEMS; BINDING MECHANISM; ESCHERICHIA-COLI; STRUCTURAL BASIS; BETA-CASEIN; PROTEIN;
D O I
10.3389/fmicb.2019.00906
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Streptococcus thermophilus, an extensively used lactic starter, is generally produced in yeast extract-based media containing a complex mixture of peptides whose exact composition remains elusive. In this work, we aimed at investigating the peptide content of a commercial yeast extract (YE) and identifying dynamics of peptide utilization during the growth of the industrial S. thermophilus N4L strain, cultivated in 1 l bioreactors under pH-regulation. To reach that goal, we set up a complete analytical workflow based on mass spectrometry (peptidomics). About 4,600 different oligopeptides ranging from 6 to more than 30 amino acids in length were identified during the time-course of the experiment. Due to the low spectral abundance of individual peptides, we performed a clustering approach to decipher the rules of peptide utilization during fermentation. The physicochemical characteristics of consumed peptides perfectly matched the known affinities of the oligopeptide transport system of S. thermophilus. Moreover, by analyzing such a large number of peptides, we were able to establish that peptide net charge is the major factor for oligopeptide transport in S. thermophilus N4L.
引用
收藏
页数:12
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