ArticleApplied and environmental microbiology2005
Identification of endopeptidase genes from the genomic sequence of Lactobacillus helveticus CNRZ32 and the role of these genes in hydrolysis of model bitter peptides.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 61 citations in OpenAlex.
- The Enzyme Gene Expression of Protein Utilization and Metabolism byMicroorganisms · 2022Article
- Metabolism Characteristics of Lactic Acid Bacteria and the Expanding Applications in Food Industry.Frontiers in bioengineering and biotechnology · 2021Review
- Effects of UPR and ERAD pathway on the prolyl endopeptidase production in Pichia pastoris by controlling of nitrogen source.Journal of industrial microbiology & biotechnology · 2017Article
- Dipeptidase activity and growth of heat-treated commercial dairy starter culture.Applied biochemistry and biotechnology · 2015Article
- Cloning and expression of a novel prolyl endopeptidase from Aspergillus oryzae and its application in beer stabilization.Journal of industrial microbiology & biotechnology · 2015Article
- Purification and characterization of a prolyl endopeptidase isolated from Aspergillus oryzae.Journal of industrial microbiology & biotechnology · 2014Article
- Gene cloning and enzymatic characterization of an endoprotease Endo-Pro-Aspergillus niger.Journal of industrial microbiology & biotechnology · 2013Article
- Article
- Crucial role for insertion sequence elements in Lactobacillus helveticus evolution as revealed by interstrain genomic comparison.Applied and environmental microbiology · 2010Article
- Genome sequence and comparative genome analysis of Lactobacillus casei: insights into their niche-associated evolution.Genome biology and evolution · 2009Article
- Comparative genomics of lactic acid bacteria reveals a niche-specific gene set.BMC microbiology · 2009Article
- Characterization of the pattern of alphas1- and beta-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581.Applied and environmental microbiology · 2008Article
- Phenotypic and genotypic analysis of amino acid auxotrophy in Lactobacillus helveticus CNRZ 32.Applied and environmental microbiology · 2008Article
- Genome sequence of Lactobacillus helveticus, an organism distinguished by selective gene loss and insertion sequence element expansion.Journal of bacteriology · 2008Article
- Comparative high-density microarray analysis of gene expression during growth of Lactobacillus helveticus in milk versus rich culture medium.Applied and environmental microbiology · 2007Article
- Response of Lactobacillus helveticus PR4 to heat stress during propagation in cheese whey with a gradient of decreasing temperatures.Applied and environmental microbiology · 2006Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genes encoding three putative endopeptidases were identified from a draft-quality genome sequence of Lactobacillus helveticus CNRZ32 and designated pepO3, pepF, and pepE2. The ability of cell extracts from Escherichia coli DH5alpha derivatives expressing CNRZ32 endopeptidases PepE, PepE2, PepF, PepO, PepO2, and PepO3 to hydrolyze the model bitter peptides, beta-casein (beta-CN) (f193-209) and alpha(S1)-casein (alpha(S1)-CN) (f1-9), under cheese-ripening conditions (pH 5.1, 4% NaCl, and 10 degrees C) was examined. CNRZ32 PepO3 was determined to be a functional paralog of PepO2 and hydrolyzed both peptides, while PepE and PepF had unique specificities towards alpha(S1)-CN (f1-9) and beta-CN (f193-209), respectively. CNRZ32 PepE2 and PepO did not hydrolyze either peptide under these conditions. To demonstrate the utility of these peptidases in cheese, PepE, PepO2, and PepO3 were expressed in Lactococcus lactis, a common cheese starter, using a high-copy vector pTRKH2 and under the control of the pepO3 promoter. Cell extracts of L. lactis derivatives expressing these peptidases were used to hydrolyze beta-CN (f193-209) and alpha(S1)-CN (f1-9) under cheese-ripening conditions in single-peptide reactions, in a defined peptide mix, and in Cheddar cheese serum. Peptides alpha(S1)-CN (f1-9), alpha(S1)-CN (f1-13), and alpha(S1)-CN (f1-16) were identified from Cheddar cheese serum and included in the defined peptide mix. Our results demonstrate that in all systems examined, PepO2 and PepO3 had the highest activity with beta-CN (f193-209) and alpha(S1)-CN (f1-9). Cheese-derived peptides were observed to affect the activity of some of the enzymes examined, underscoring the importance of incorporating such peptides in model systems. These data indicate that L. helveticus CNRZ32 endopeptidases PepO2 and PepO3 are likely to play a key role in this strain's ability to reduce bitterness in cheese.
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