Characterization of the mature cell surface proteinase of Lactobacillus delbrueckii subsp. lactis CRL 581

Villegas, Josefina M.; Brown, Lucía; Giori, Graciela Savoy de; Hébert, Elvira María

doi:10.1007/s00253-014-6258-6

Cited by 19 publications

(31 citation statements)

References 44 publications

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“…lactis . (Kunji et al., 1996; Savijoki et al., 2006; Villegas, Brown, De Giori, & Hebert, 2015). Aside these, CEPs have also been reported in some strains of various LAB species such as Lb.…”

Section: Types Of Cepsmentioning

confidence: 99%

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

et al. 2020

Comp Rev Food Sci Food Safe

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Proteins displayed on the cell surface of lactic acid bacteria (LAB) perform diverse and important biochemical roles. Among these, the cell‐envelope proteinases (CEPs) are one of the most widely studied and most exploited for biotechnological applications. CEPs are important players in the proteolytic system of LAB, because they are required by LAB to degrade proteins in the growth media into peptides and/or amino acids required for the nitrogen nutrition of LAB. The most important area of application of CEPs is therefore in protein hydrolysis, especially in dairy products. Also, the physical location of CEPs (i.e., being cell‐envelope anchored) allows for relatively easy downstream processing (e.g., extraction) of CEPs. This review describes the biochemical features and organization of CEPs and how this fits them for the purpose of protein hydrolysis. It begins with a focus on the genetic organization and expression of CEPs. The catalytic behavior and cleavage specificities of CEPs from various LAB are also discussed. Following this, the extraction and purification of most CEPs reported to date is described. The industrial applications of CEPs in food technology, health promotion, as well as in the growing area of water purification are discussed. Techniques for improving the production and catalytic efficiency of CEPs are also given an important place in this review.

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Section: Types Of Cepsmentioning

confidence: 99%

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

et al. 2020

Comp Rev Food Sci Food Safe

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“…Overall, these evidences support that the observed CEP activities could be due to the mixed PI/PIII-type proteases. PI/PIII-type proteases have been characterized in lactobacilli (Fernandez de Palencia et al, 1997;Sadat-Mekmene et al, 2011aVillegas et al, 2015 and lactococci (Nikolić, Tolinački, Fira, Golić, & Topisirović, 2009). In particular, like PRA331, Lb.…”

Section: Peptidomic Analysis Of Milk Fermented With Lactobacillus Casmentioning

confidence: 99%

Peptidomic study of casein proteolysis in bovine milk by Lactobacillus casei PRA205 and Lactobacillus rhamnosus PRA331

Solieri

Vero

Tagliazucchi

2018

International Dairy Journal

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Lactobacilli contain different cell envelope proteinases (CEPs) responsible for the hydrolysis of caseins and the release of various bioactive peptides. In this work, we explored the CEP activity of Lactobacillus casei PRA205 and Lactobacillus rhamnosus PRA331 whole cells towards β-, αS1-, κand αS2-caseins in bovine milk. Mass spectrometry analysis of fermented milk hydrolysates identified a total of 331 peptides, which were mainly derived from β-caseins (59.0 and 60.1% for PRA205 and PRA331, respectively). The analysis of αS1-casein (f1-23) cleavage site specificity congruently supports that Lb. casei PRA205 and Lb. rhamnosus PRA331 exhibited a mixed-type CEPI/III activity. PRA205 and PRA331 CEPs also showed cleavage site specificity toward β-casein, preferentially. These CEPs cleaved the peptide bond preferentially when hydrophobic or negatively charged amino acids were present. 13.5% and 13.7% of peptides released by Lb. casei PRA205 and Lb. rhamnosus PRA331 CEPs were found to have 100% homology with previously identified bioactive peptides.

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“…delbrueckii subsp. lactis CRL 581 was sequenced and only one gene encoding a CEP, named PrtL was detected 11 , 16 . In contrast to Lc .…”

Section: Resultsmentioning

confidence: 99%

“…This proteolytic system consists of (i) an extracellular cell envelope-associated proteinase (CEP) that hydrolyzes caseins into oligopeptides; (ii) specialized transport systems that take up peptides into the cell; and (iii) several intracellular peptidases, which degrade peptides into amino acids 2 , 8 , 9 . Furthermore, this proteolytic system contributes to the flavor and texture development of fermented products 9 , 10 , and may release bioactive health-beneficial peptides during milk fermentation 8 – 11 .…”

Section: Introductionmentioning

confidence: 99%

“…delbrueckii subsp. lactis CRL 581, a strain isolated from a homemade Argentinian hard cheese, possesses a CEP (PrtL) that is able to release a series of bioactive health-beneficial peptides (i.e., anti-inflammatory, antihypertensive, and phosphopeptides) from α- and β-caseins 11 , 12 . It was observed that the production of bioactive peptides by PrtL was repressed by the peptide content of the growth medium 7 .…”

Section: Introductionmentioning

confidence: 99%

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YebC, a putative transcriptional factor involved in the regulation of the proteolytic system of Lactobacillus

Brown

Villegas

Elean

et al. 2017

Sci Rep

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The proteolytic system of Lactobacillus plays an essential role in bacterial growth, contributes to the flavor development of fermented products, and can release bioactive health-beneficial peptides during milk fermentation. In this work, a genomic analysis of all genes involved in the proteolytic system of L. delbrueckii subsp. lactis CRL 581 was performed. Genes encoding the cell envelope-associated proteinase, two peptide transport systems, and sixteen peptidases were identified. The influence of the peptide supply on the transcription of 23 genes involved in the proteolytic system of L. delbrueckii subsp. lactis was examined after cell growth in a chemically defined medium (CDM) and CDM supplemented with Casitone. prtL, oppA 1, optS, optA genes as well as oppDFBC and optBCDF operons were the most highly expressed genes in CDM; their expression being repressed 6- to 115-fold by the addition of peptides. The transcriptional analysis was confirmed by proteomics; the up-regulation of the PrtL, PepG, OppD and OptF proteins in the absence of peptides was observed while the DNA-binding protein YebC was up-regulated by peptides. Binding of YebC to the promoter region of prtL, oppA 1, and optS, demonstrated by electrophoretic mobility shift assays, showed that YebC acts as a transcriptional repressor of key proteolytic genes.

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Characterization of the mature cell surface proteinase of Lactobacillus delbrueckii subsp. lactis CRL 581

Cited by 19 publications

References 44 publications

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

Peptidomic study of casein proteolysis in bovine milk by Lactobacillus casei PRA205 and Lactobacillus rhamnosus PRA331

YebC, a putative transcriptional factor involved in the regulation of the proteolytic system of Lactobacillus

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