Editing of the Proteolytic System of Lactococcus lactis Increases Its Bioactive Potential

Applied and Environmental Microbiology
Chenxi Huang, Jan Kok

Abstract

Large-scale mass spectrometry-based peptidomics for bioactive-peptide discovery is relatively unexplored because of challenges in intracellular peptide extraction and small-peptide identification. Here, we present an analytical pipeline for large-scale intracellular peptidomics of Lactococcus lactis It entails an optimized sample preparation protocol for L. lactis, used as an "enzyme complex" to digest β-casein, an extraction method for its intracellular peptidome, and a peptidomics data analysis and visualization procedure. In addition, we proofread the publicly available bioactive-peptide databases and obtained an optimized database of bioactive peptides derivable from bovine β-casein. We used the pipeline to examine cultures of L. lactis MG1363 and a set of 6 isogenic multiple peptidase mutants incubated with β-casein. We observed a clearly strain-dependent accumulation of peptides with several bioactivities, such as angiotensin-converting enzyme (ACE)-inhibitory, dipeptidyl peptidase 4 (DPP-IV)-inhibitory, and immunoregulatory functions. The results suggest that both the number of different bioactive peptides and the bioactivity diversity can be increased by editing the proteolytic system of L. lactis This comprehensive pip...Continue Reading

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Citations

Aug 5, 2021·Applied and Environmental Microbiology·Fanny CanonValérie Gagnaire

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Datasets Mentioned

BETA
GM17

Methods Mentioned

BETA
gene knockout
PCR
PCRs

Software Mentioned

MS Amanda
MaxQuant
Quick
PEAKS studio
R
OMSSA
! Tandem
MyriMatch
UpSetR
R package “ alakazam ”

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