ArticleApplied and environmental microbiology2011
Simultaneous presence of PrtH and PrtH2 proteinases in Lactobacillus helveticus Strains improves breakdown of the pure alphas1-casein.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 69 citations in OpenAlex.
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- Insights on the bacterial composition of Parmigiano Reggiano Natural Whey Starter by a culture-dependent and 16S rRNA metabarcoding portrait.Scientific reports · 2022Article
- The Enzyme Gene Expression of Protein Utilization and Metabolism byMicroorganisms · 2022Article
- Little Impact of NaCl Reduction in Swiss-Type Cheese.Frontiers in nutrition · 2022Article
- Comparative Peptidomics Analysis of Fermented Milk byFoods (Basel, Switzerland) · 2021Article
- The Impact of the Adjunct Heat-Treated Starter Culture andAnimals : an open access journal from MDPI · 2021Article
- [Effect of sample preparation on analysis of human milk endogenous peptides using liquid chromatography-tandem mass spectrometry].Se pu = Chinese journal of chromatography · 2021Article
- Use of Mass Spectrometry to Profile Peptides in Whey Protein Isolate Medium Fermented byFrontiers in nutrition · 2019Article
- Distribution of Cell Envelope Proteinases Genes among Polish Strains of Lactobacillus helveticus.Polish journal of microbiology · 2018Article
- Production of Bioactive Peptides byFrontiers in microbiology · 2018Review
- κ-Casein as a source of short-chain bioactive peptides generated byJournal of food science and technology · 2017Article
- The S-layer Associated Serine Protease Homolog PrtX Impacts Cell Surface-Mediated Microbe-Host Interactions ofFrontiers in microbiology · 2017Article
- Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563.Korean journal for food science of animal resources · 2015Article
- The naturally competent strain Streptococcus thermophilus LMD-9 as a new tool to anchor heterologous proteins on the cell surface.Microbial cell factories · 2014Article
- Lactobacillus helveticus: the proteolytic system.Frontiers in microbiology · 2013Article
- The fast milk acidifying phenotype of Streptococcus thermophilus can be acquired by natural transformation of the genomic island encoding the cell-envelope proteinase PrtS.Microbial cell factories · 2011Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactobacillus helveticus can possess one or two cell envelope proteinases (CEPs), called PrtH2 and PrtH. The aim of this work was to explore the diversity of 15 strains of L. helveticus, isolated from various origins, in terms of their proteolytic activities and specificities on pure caseins or on milk casein micelles. CEP activity differed 14-fold when the strains were assayed on a synthetic substrate, but no significant differences were detected between strains possessing one or two CEPs. No correlation was observed between the proteolytic activities of the strains and their rates of acidification in milk. The kinetics of hydrolysis of purified α(s1)- and β-casein by L. helveticus whole cells was monitored using Tris-Tricine sodium dodecyl sulfate (SDS) electrophoresis, and for four strains, the peptides released were identified using mass spectrometry. While rapid hydrolysis of pure β-casein was observed for all strains, the hydrolysis kinetics of α(s1)-casein was the only criterion capable of distinguishing between the strains based on the number of CEPs. Fifty-four to 74 peptides were identified for each strain. When only PrtH2 was present, 22 to 30% of the peptides originated from α(s1)-casein. The percentage increased to 41 to 49% for strains in which both CEPs were expressed. The peptide size ranged from 6 to 33 amino acids, revealing a broad range of cleavage specificities, involving all classes of amino acids (Leu, Val, Ala, Ile, Glu, Gln, Lys, Arg, Met, and Pro). Regions resistant to proteolysis were identified in both caseins. When strains were grown in milk, a drastic reduction in the number of peptides was observed, reflecting changes in accessibility and/or peptide assimilation during growth.
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