ArticleApplied and environmental microbiology2005
Enzymatic ability of Bifidobacterium animalis subsp. lactis to hydrolyze milk proteins: identification and characterization of endopeptidase O.
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. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 66 citations in OpenAlex.
- Comparison of Physicochemical, Microbiological, and Sensory Properties of Yogurt Made From Cow, Goat, Sheep, and Buffalo Milk with and Without Probiotic Cultures.Food science & nutrition · 2026Article
- Soybean Protein Hydrolysate Enhances Growth and Freeze-Drying Survival ofFoods (Basel, Switzerland) · 2025Article
- Environmental factors drive bacterial degradation of gastrointestinal mucus.NPJ biofilms and microbiomes · 2025Article
- Bifidobacteria in Fermented Dairy Foods: A Health Beneficial Outlook.Probiotics and antimicrobial proteins · 2025Review
- A study on antimicrobial activity of lysine-like peptoids for the development of new antimicrobials.Archives of microbiology · 2025Article
- Article
- In Silico Predictions of Ecological Plasticity Mediated by Protein Family Expansions in Early-Diverging Fungi.Journal of fungi (Basel, Switzerland) · 2022Article
- Casomorphins and Gliadorphins Have Diverse Systemic Effects Spanning Gut, Brain and Internal Organs.International journal of environmental research and public health · 2021Article
- Properties of recombinant 4-α-glucanotransferase fromFood science and biotechnology · 2020Article
- Bifidobacteria and Their Health-Promoting Effects.Microbiology spectrum · 2017Review
- Screening of Bifidobacteria and Lactobacilli Able to Antagonize the Cytotoxic Effect of Clostridium difficile upon Intestinal Epithelial HT29 Monolayer.Frontiers in microbiology · 2016Article
- Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity.Frontiers in microbiology · 2016Article
- Milk Intolerance, Beta-Casein and Lactose.Nutrients · 2015Review
- Characterization of a New M13 Metallopeptidase from Deep-Sea Shewanella sp. E525-6 and Mechanistic Insight into Its Catalysis.Frontiers in microbiology · 2015Article
- 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
- Detection of Bifidobacterium animalis subsp. lactis (Bb12) in the intestine after feeding of sows and their piglets.Applied and environmental microbiology · 2008Article
- Characterization of a Bifidobacterium longum BORI dipeptidase belonging to the U34 family.Applied and environmental microbiology · 2007Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteolytic system of Bifidobacterium animalis subsp. lactis was analyzed, and an intracellular endopeptidase (PepO) was identified and characterized. This work reports the first complete cloning, purification, and characterization of a proteolytic enzyme in Bifidobacterium spp. Aminopeptidase activities (general aminopeptidases, proline iminopeptidase, X-prolyl dipeptidylaminopeptidase) found in cell extracts of B. animalis subsp. lactis were higher for cells that had been grown in a milk-based medium than for those grown in MRS. A high specific proline iminopeptidase activity was observed in B. animalis subsp. lactis. Whole cells and cell wall-bound protein fractions showed no caseinolytic activity; however, the combined action of intracellular proteolytic enzymes could hydrolyze casein fractions rapidly. The endopeptidase activity of B. animalis subsp. lactis was examined in more detail, and the gene encoding an endopeptidase O in B. animalis subsp. lactis was cloned and overexpressed in Escherichia coli. The deduced amino acid sequence for B. animalis subsp. lactis PepO indicated that it is a member of the M13 peptidase family of zinc metallopeptidases and displays 67.4% sequence homology with the predicted PepO protein from Bifidobacterium longum. The recombinant enzyme was shown to be a 74-kDa monomer. Activity of B. animalis subsp. lactis PepO was found with oligopeptide substrates of at least 5 amino acid residues, such as met-enkephalin, and with larger substrates, such as the 23-amino-acid peptide alpha s1-casein(f1-23). The predominant peptide bond cleaved by B. animalis subsp. lactis PepO was on the N-terminal side of phenylalanine residues. The enzyme also showed a post-proline secondary cleavage site.
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