Cloning, characterization, expression and antifungal activity of an alkaline serine protease of Aureobasidium pullulans PL5 involved in the biological control of postharvest pathogens
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An alkaline protease gene was amplified from genomic DNA and cDNA of the antagonistic yeast-like fungus Aureobasidium pullulans PL5, a biocontrol agent effective against Monilinia laxa on stone fruit and Botrytis cinerea and Penicillium expansum on pome fruits. An open reading frame of 1248 bp encoding a 415-amino acid (aa) protein with a calculated molecular weight (M(r)) of 42.9 kDa and an isoelectric point (pI) of 4.5 was characterized. The cDNAALP5 gene had an 18-amino acid signal peptide, one N-gylcosylation, one histidine active site, and one serine active site. The ALP5 gene with a M(r) of 1351 bp contained two introns. One intron was of 54 bp, while the other was of 50 bp. Protein BLAST and phylogenetic tree analysis of the deduced amino sequences from the cDNAALP5 gene showed that the encoded protein had 100% homology to a protease enzyme (ALP2) of a sea strain of A. pullulans, suggesting that the protein ALP5 was an alkaline serine protease. Expression of ALP5 in Escherichia coli BL21 (DE3), followed by identification with Western-blotting, purification with Ni-NTA and analysis of enzymatic activity, yielded an homogeneous recombinant ALP5 which hydrolysed the substrate casein and inhibited the mycelial growth of the pathogens. At its optimal pH of 10.0 and reaction temperature of 50°C, the recombinant protease exhibited the highest activity towards the substrate casein, though the highest stability was at lower temperatures and pH between 7.0 and 9.0. This study provided the direct evidence that extracellular proteases secreted by the antagonist A. pullulans PL5 played a role in the biocontrol activities against some postharvest pathogens of apple and peach.
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The alkaline serine protease Alp5 from A. pullulans reduced spore germination and germ tube length of Penicillium expansum, B. cinerea, M. fructicola and Alternaria alternata in vitro and exhibited a concentration-dependent inhibitory effect on these pathogens on apple.
“In contrast, the alkaline serine protease Alp5 from A. pullulans reduced spore germination and germ tube length of Penicillium expansum, B. cinerea, M. fructicola and Alternaria alternata in vitro and exhibited a concentration-dependent inhibitory effect on these pathogens on apple (Banani et al. 2014; Zhang et al. 2012).”
From Biocontrol yeasts: mechanisms and applications (2019) · cites this paper as Zhang et al. 2012
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- Authors
- Zhang, D., Spadaro, D., Valente, S., Garibaldi, A., & Gullino, M. L.
- Affiliations
- University of Turin (IT)
- Corresponding author
- Spadaro, Davide
- Venue
- International Journal of Food Microbiology
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 153
- Issue
- 3
- Pages
- 453-464
- ISSN
- 0168-1605 (ISSN-L)
- OpenAlex
- W2080548543
- Cited by
- 87
- References
- 61
- Citations by year
- 2026: 7 · 2025: 4 · 2024: 8 · 2023: 12 · 2022: 7 · 2021: 7 · 2020: 8 · 2019: 6 · 2018: 9 · 2017: 2 · 2016: 3 · 2015: 5 · 2014: 7 · 2013: 2
- FWCI
- 3.23
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- International Journal of Food Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System University of Turin (University of Turin) (submittedVersion, other-oa)
- Funders
- Ministero dell’Istruzione, dell’Università e della Ricerca
- Regione Piemonte
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Postharvest Quality and Shelf Life Management
- Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Fungal Plant Pathogen Control
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- alkaline serine protease, antifungal activity, biological control, postharvest pathogens, Monilinia laxa, Botrytis cinerea, Penicillium expansum, enzyme characterization, apple, peach, introns
- MeSH terms
- Amino Acid Sequence, Animals, Ascomycota, Bacterial Proteins, Base Sequence, Cloning, Molecular, Escherichia coli, Fruit, Hydrolysis, Introns, Molecular Sequence Data, Penicillium, Endopeptidases, Phylogeny, Serine, Serine Endopeptidases, Open Reading Frames, Sequence Homology, DNA, Complementary, Cloning, Organism, Botrytis, Serine Proteases, Biological Control Agents
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