ArticleApplied and environmental microbiology2003
Purification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii.
Article in Applied and environmental microbiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 61 citations in OpenAlex.
- Isolation of Debaryomyces hansenii and selection of an optimal strain to improve the quality of low-grade beef rump (middle gluteal) during dry aging.Animal bioscience · 2023Article
- Yeasts Inhabiting Extreme Environments and Their Biotechnological Applications.Microorganisms · 2022Review
- Intracellular Aminopeptidase Activity Determination from the Fungus Sporisorium reilianum: Purification and Biochemical Characterization of psrAPEi Enzyme.Current microbiology · 2022Article
- Therapeutic and biotechnological applications of substrate specific microbial aminopeptidases.Applied microbiology and biotechnology · 2020Review
- Optimized expression of prolyl aminopeptidase in Pichia pastoris and its characteristics after glycosylation.World journal of microbiology & biotechnology · 2016Article
- Article
- Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.The protein journal · 2015Article
- Evidence for the Existence in Arabidopsis thaliana of the Proteasome Proteolytic Pathway: ACTIVATION IN RESPONSE TO CADMIUM.The Journal of biological chemistry · 2009Article
- Characterization of a multimeric, eukaryotic prolyl aminopeptidase: an inducible and highly specific intracellular peptidase from the non-pathogenic fungus Talaromyces emersonii.Microbiology (Reading, England) · 2009Article
- Interaction of a self-assembling peptide with oligonucleotides: complexation and aggregation.Biophysical journal · 2007Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A prolyl aminopeptidase (PAP) (EC 3.4.11.5) was isolated from the cell extract of Debaryomyces hansenii CECT12487. The enzyme was purified by selective fractionation with protamine and ammonium sulfate, followed by two chromatography steps, which included gel filtration and anion-exchange chromatography. The PAP was purified 248-fold, with a recovery yield of 1.4%. The enzyme was active in a broad pH range (from 5 to 9.5), with pH and temperature optima at 7.5 and 45 degrees C. The molecular mass was estimated to be around 370 kDa. The presence of inhibitors of serine and aspartic proteases, bestatin, puromycin, reducing agents, chelating agents, and different cations did not have any effect on the enzyme activity. Only iodoacetate, p-chloromercuribenzoic acid, and Hg(2+), which are inhibitors of cysteine proteases, markedly reduced the enzyme activity. The K(m) for proline-7-amido-4-methylcoumarin was 40 micro M. The enzyme exclusively hydrolyzed N-terminal-proline-containing substrates. This is the first report on the identification and purification of this type of aminopeptidase in yeast, which may contribute to the scarce knowledge about D. hansenii proteases and their possible roles in meat fermentation.
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