ArticleJournal of industrial microbiology & biotechnology2013
Gene cloning and enzymatic characterization of an endoprotease Endo-Pro-Aspergillus niger.
Article in Journal of industrial microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- High-level production of Aspergillus niger prolyl endopeptidase from agricultural residue and its application in beer brewing.Microbial cell factories · 2023Article
- Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications.Plants (Basel, Switzerland) · 2022Review
- Gluten-degrading bacteria: availability and applications.Applied microbiology and biotechnology · 2021Review
- Bioinformatic mapping of a more precise Aspergillus niger degradome.Scientific reports · 2021Article
- 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
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Authors and funding
3 authors.
Funding
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Abstract
A novel endoprotease Endo-Pro-Aspergillus niger (endoprotease EPR) was first successfully expressed at high level in the methylotrophic yeast Pichia pastoris and the purification procedure was established. The endoprotease EPR is 95 % identity with proline specific endopeptidase from A. niger CBS513.88 (EMBL; AX458699), while sharing low identity with those from other microorganisms. The purified endoprotease EPR was a monomer of 60 kDa. Furthermore, the peptide mass fingerprinting (PMF) analysis confirmed that the purified protein was an endoprotease Endo-Pro-Aspergillus niger. A three-dimensional model revealed that the active site of the enzyme was located in Ser(179)-Asp(458)-His(491), based on template 3n2zB with sequence identity of 17.6 %. The optimum pH and temperature of the endoprotease EPR were pH 4-5 and 35 °C, and the stabilities were pH 3-7 and 15-60 °C, respectively. Furthermore, the endoprotease EPR had the ability to digest peptides with the C-terminal of proline as well as alanine, and was also capable of hydrolyzing larger peptides. The properties of the endoprotease EPR made it a highly promising candidate for future application in the field of brewing and food process.
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Registered trials
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