ArticlePloS one2013
Characterization of the recombinant exopeptidases PepX and PepN from Lactobacillus helveticus ATCC 12046 important for food protein hydrolysis.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 65 citations in OpenAlex.
- Genomic and Proteolytic Profiling of Lacticaseibacillus sp. PRA205: Insights into PepX-Mediated Bioactive Peptide Metabolism.Probiotics and antimicrobial proteins · 2026Article
- Enhancing leucine aminopeptidase activity in Aspergillus oryzae LL1 through multi-round UV irradiation mutagenesis with potential application in debittering.Biotechnology letters · 2025Article
- Association of Gut Microbiome and Dipeptidyl Peptidase 4 in Immune-Mediated Inflammatory Bowel Disease: A Rapid Literature Review.International journal of molecular sciences · 2024Review
- Gut microbiota DPP4-like enzymes are increased in type-2 diabetes and contribute to incretin inactivation.Genome biology · 2024Article
- Comparative Binding Study of Gliptins to Bacterial DPP4-like Enzymes for the Treatment of Type 2 Diabetes Mellitus (T2DM).International journal of molecular sciences · 2024Article
- Elucidating the Role of a Calcium-Binding Loop in anACS omega · 2023Article
- Enhanced Molecular Networking ShowsMarine drugs · 2023Article
- Technological Characterization of Lactic Acid Bacteria Strains for Potential Use in Cheese Manufacture.Foods (Basel, Switzerland) · 2023Article
- A novel aminopeptidase with potential debittering properties in casein and soybean protein hydrolysates.Food science and biotechnology · 2020Article
- Therapeutic and biotechnological applications of substrate specific microbial aminopeptidases.Applied microbiology and biotechnology · 2020Review
- Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus.Acta crystallographica. Section F, Structural biology communications · 2019Article
- The DPP-4 inhibitor vildagliptin impacts the gut microbiota and prevents disruption of intestinal homeostasis induced by a Western diet in mice.Diabetologia · 2018Article
- Commentary: The Potential Role of the Dipeptidyl Peptidase-4-Like Activity From the Gut Microbiota on the Host Health.Frontiers in microbiology · 2018Article
- The Potential Role of the Dipeptidyl Peptidase-4-Like Activity From the Gut Microbiota on the Host Health.Frontiers in microbiology · 2018Article
- A Novel Glutamyl (Aspartyl)-Specific Aminopeptidase A from Lactobacillus delbrueckii with Promising Properties for Application.PloS one · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proline-specific X-prolyl dipeptidyl aminopeptidase (PepX; EC 3.4.14.11) and the general aminopeptidase N (PepN; EC 3.4.11.2) from Lactobacillus helveticus ATCC 12046 were produced recombinantly in E. coli BL21(DE3) via bioreactor cultivation. The maximum enzymatic activity obtained for PepX was 800 µkat(H-Ala-Pro-pNA) L(-1), which is approx. 195-fold higher than values published previously. To the best of our knowledge, PepN was expressed in E. coli at high levels for the first time. The PepN activity reached 1,000 µkat(H-Ala-pNA) L(-1). After an automated chromatographic purification, both peptidases were biochemically and kinetically characterized in detail. Substrate inhibition of PepN and product inhibition of both PepX and PepN were discovered for the first time. An apo-enzyme of the Zn(2+)-dependent PepN was generated, which could be reactivated by several metal ions in the order of Co(2+)>Zn(2+)>Mn(2+)>Ca(2+)>Mg(2+). PepX and PepN exhibited a clear synergistic effect in casein hydrolysis studies. Here, the relative degree of hydrolysis (rDH) was increased by approx. 132%. Due to the remarkable temperature stability at 50°C and the complementary substrate specificities of both peptidases, a future application in food protein hydrolysis might be possible.
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