Use of a free form of the Streptococcus thermophilus cell envelope protease PrtS as a tool to produce bioactive peptides

Chang, Oun Ki; Roux, Émeline; Awussi, Ahoefa Ablavi; Miclo, Laurent; Jardin, Julien; Jameh, Nawara; Dary, Annie; Humbert, G.; Perrin, Clarisse

doi:10.1016/j.idairyj.2014.01.008

Cited by 36 publications

(43 citation statements)

References 46 publications

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“…The reason for the different cleavage patterns might be that the structure of α s1 -CN was changed during fermentation in milk to make it more accessible for hydrolysis by B. longum . A similar result was reported by Chang et al (2014) and Sadat-Mekmene et al (2011b) , who also found that the proteases PrtS and PrtH of S. thermophilus and L. helveticus , respectively, were more accessible at the N terminus than the C terminus.…”

Section: Resultssupporting

confidence: 88%

“…As shown in Table 2 , the peptides in the fermentate were identified to have been generated from CN. The results also indicated that CN was the preferential substrate of B. longum in spite of the presence of whey protein in skim milk, similar to a strain of St. thermophilus ( Chang et al , 2014 ). A total of 28 peptides were generated, corresponding to 11 β-CN, 16 α s1 -CN, and 1 κ-CN peptide.…”

Section: Resultsmentioning

confidence: 71%

“…On the other hand, the N terminus of β-CN was resistant to hydrolysis by B. longum , as previously reported by Chang et al (2013) . The C terminus of β-CN, which was determined to be a hydrophobic region in this study, is more accessible for hydrolysis by B. longum ( Chang et al , 2013 ) and by the proteases of S. thermophilus ( Chang et al , 2014 ; Miclo et al , 2012 ) and L. helveticus ( Sadat-Mekmene et al , 2011a ).…”

Section: Resultsmentioning

confidence: 92%

“…Liquid chromatography-electrospray ionization-quantitative time-of-flight tandem mass spectrometry experiments (LC-ESI-TOF-MS/MS) were performed at the National Instrumentation Center for Environmental Management (NICEM) of Seoul National University in Korea, according to the method described by Chang et al (2013) .…”

Section: Methodsmentioning

confidence: 99%

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Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563

Ha¹,

Chang²,

Jo³

et al. 2015

Korean Journal for Food Science of Animal Resources

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Angiotensin-converting enzyme (ACE) inhibitory activity was evaluated for the low-molecular-weight fraction (<3 kDa) obtained from milk fermentation by Bifidobacterium longum KACC91563. The ACE inhibitory activity in this fraction was 62.3%. The peptides generated from the <3 kDa fraction were identified by liquid chromatography-electrospray ionization quantitative time-of-flight mass spectrometry analysis. Of the 28 peptides identified, 11 and 16 were identified as β-casein (CN) and αs1-CN, respectively. One peptide was identified as κ-CN. Three peptides, YQEPVLGPVRGPFPIIV, QEPVLGPVRGPFPIIV, and GPVRGPFPIIV, from β-CN corresponded to known antihypertensive peptides. We also found 15 peptides that were identified as potential antihypertensive peptides because they included a known antihypertensive peptide fragment. These peptides were as follows: RELEELNVPGEIVE (f1-14), YQEPVLGPVRGPFP (f193-206), EPVLGPVRGPFPIIV (f195-206), PVLGPVRGPFPIIV (f196-206), VLGPVRGPFPIIV (f197-206), and LGPVRGPFPIIV (f198-206) for β-CN; and APSFSDIPNPIGSENSEKTTMPLW (f176-199), SFSDIPNPIGSENSEKT- TMPLW (f178-199), FSDIPNPIGSENSEKTTMPLW (f179-199), SDIPNPIGSENSEKTTMPLW (f180-199), DIPNPIGSENSEKTTMPLW (f181-199), IPNPIGSENSEKTTMPLW (f182-199), PIGSENSEKTTMPLW (f185-199), IGSENSEKTTMPLW (f186-199), and SENSEKTTMPLW (f188-199) for αs1-CN. From these results, B. longum could be used as a starter culture in combination with other lactic acid bacteria in the dairy industry, and/or these peptides could be used in functional food manufacturing as additives for the development of a product with beneficial effects for human health.

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 71%

Section: Resultsmentioning

confidence: 92%

Section: Methodsmentioning

confidence: 99%

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Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563

Ha¹,

Chang²,

Jo³

et al. 2015

Korean Journal for Food Science of Animal Resources

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“…The LAB Streptococcus thermophilus is the second most important species of industrial dairy starter after Lactococcus lactis and is widely used in the manufacture of various dairy products such as yogurt and hard cooked cheeses (Hols et al, 2005), mainly for its fast acidification (Dandoy et al, 2011) and organoleptic properties. Moreover, some strains of S. thermophilus have the capacity to generate a variety of bioactive peptides from milk caseins owing to its proteolytic system (Miclo et al, 2012;Chang et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

The X-prolyl dipeptidyl-peptidase PepX of Streptococcus thermophilus initially described as intracellular is also responsible for peptidase extracellular activity

Hafeez

Cakir-Kiefer

Lecomte

et al. 2019

Journal of Dairy Science

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This study addresses the hypothesis that the extracellular cell-associated X-prolyl dipeptidyl-peptidase activity initially described in Streptococcus thermophilus could be attributable to the intracellular X-prolyl dipeptidyl-peptidase PepX. For this purpose, a PepXnegative mutant of S. thermophilus LMD-9 was constructed by interrupting the pepX gene and named LMD-9-∆pepX. When cultivated, the S. thermophilus LMD-9 wild type strain grew more rapidly than its ∆pepX mutant counterpart. Thus, the growth rate of the LMD-9-∆pepX strain was reduced by a factor of 1.5 and 1.6 in milk and LM17 medium (M17 medium supplemented with 2% lactose), respectively. The negative effect of the PepX inactivation on the hydrolysis of β-casomorphin-7 was also observed. Indeed, when incubated with this peptide, the LMD-9-∆pepX mutant cells were unable to hydrolyze it, whereas this peptide was completely degraded by the S. thermophilus LMD-9 wild type cells. This hydrolysis was not due to leakage of intracellular PepX, as no peptide hydrolysis was highlighted in cell-free filtrate of wild type strain. Therefore, based on these results, it can be presumed that though lacking an export signal, the intracellular PepX might have accessed the β-casomorphin-7 externally, perhaps via its galactose-binding domain-like fold, this domain being known to help enzymes bind to several proteins and substrates. Therefore, the identification of novel distinctive features of the proteolytic system of S. thermophilus will further enhance its credibility as a starter in milk fermentation.

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Improved functionality of fermented milk is mediated by the synbiotic interaction between Cudrania tricuspidata leaf extract and Lactobacillus gasseri strains

Oh¹,

Lee

et al. 2016

Appl Microbiol Biotechnol

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This study was designed to investigate the cooperative effect of selected Lactobacillus gasseri strains and Cudrania tricuspidata (CT) leaf extract in enhancing the health-promoting activities of fermented milk. Addition of CT increased total bacterial counts and proteolysis during fermentation of milk with L. gasseri strains. Antioxidant capacities were determined by measuring the ABTS, DPPH, and peroxyl radical scavenging activities and ferric reducing power. The antioxidant capacity of CT-supplemented milk was greater than that of milk without supplementation; moreover, the antioxidant activity of CT-supplemented milk was synergistically improved by fermentation with L. gasseri strains. In particular, CT-supplemented milk fermented by L. gasseri 505 showed the highest antioxidant activity. The phenolic compounds in CT, such as neo-chlorogenic, chlorogenic, and caffeic acid, were metabolized during fermentation with L. gasseri strains, and 3,4-dihydroxy-hydrocinnamic acid was produced as a fermentation metabolite. Moreover, the liberation of bioactive peptides of fermented milk was increased by the proteolytic activity of L. gasseri strains. In particular, six peptides, which were mainly derived from β-casein, were newly identified in this study. These findings suggest that L. gasseri strains metabolize the phenolic acids in the CT and the bioactive peptides released through this interaction improve the antioxidant activity of the fermented milk.

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Use of a free form of the Streptococcus thermophilus cell envelope protease PrtS as a tool to produce bioactive peptides

Cited by 36 publications

References 46 publications

Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563

Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563

The X-prolyl dipeptidyl-peptidase PepX of Streptococcus thermophilus initially described as intracellular is also responsible for peptidase extracellular activity

Improved functionality of fermented milk is mediated by the synbiotic interaction between Cudrania tricuspidata leaf extract and Lactobacillus gasseri strains

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