ArticleJournal of industrial microbiology & biotechnology2014
Purification and characterization of a prolyl endopeptidase isolated from Aspergillus oryzae.
Article in Journal of industrial microbiology & biotechnology, 2014. 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, 22 citations in OpenAlex.
- High-level production of Aspergillus niger prolyl endopeptidase from agricultural residue and its application in beer brewing.Microbial cell factories · 2023Article
- A Minimally Invasive Approach for Preventing White Wine Protein Haze by Early Enzymatic Treatment.Foods (Basel, Switzerland) · 2022Article
- A new microbial gluten-degrading prolyl endopeptidase: Potential application in celiac disease to reduce gluten immunogenic peptides.PloS one · 2019Article
- 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
- Purification, characterization, and application of a thermostable dextranase from Talaromyces pinophilus.Journal of industrial microbiology & biotechnology · 2017Article
- Cloning and expression of a novel prolyl endopeptidase from Aspergillus oryzae and its application in beer stabilization.Journal of industrial microbiology & biotechnology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new fungal strain that was isolated from our library was identified as an Aspergillus oryzae and noted to produce a novel proly endopeptidase. The enzyme was isolated, purified, and characterized. The molecular mass of the prolyl endopeptidase was estimated to be 60 kDa by using SDS-PAGE. Further biochemical characterization assays revealed that the enzyme attained optimal activity at pH 4.0 with acid pH stability from 3.0 to 5.0. Its optimum temperature was 30 °C and residual activity after 30 min incubation at 55 °C was higher than 80 %. The enzyme was activated and stabilized by Ca(2+) but inhibited by EDTA (10 mM) and Cu(2+). The K m and k cat values of the purified enzyme for different length substrates were also evaluated, and the results imply that the enzyme from A. oryzae possesses higher affinity for the larger substrates. Furthermore, this paper demonstrates for the first time that a prolyl endopeptidase purified from A. oryzae is able to hydrolyze intact casein.
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Registered trials
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