ArticleInternational microbiology : the official journal of the Spanish Society for Microbiology2021
Penicillin G acylase production by Mucor griseocyanus and the partial genetic analysis of its pga gene.
Article in International microbiology : the official journal of the Spanish Society for Microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Research progress on immobilized penicillin G acylase and industrial applications.RSC advances · 2026Review
- Effect of enzyme preparation and extrusion puffing treatment on sorghum straw silage fermentation.Scientific reports · 2024Article
- Immobilization and property of penicillin G acylase on amino functionalized magnetic NiFrontiers in bioengineering and biotechnology · 2023Article
- Exploitation of E. coli for the production of penicillin G amidase: a tool for the synthesis of semisynthetic β-lactam antibiotics.Journal, genetic engineering & biotechnology · 2021Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Penicillin acylases (penicillin amidohydrolase, EC 3.5.1.11) are a group of enzymes with many applications within the pharmaceutical industry, and one of them is the production of semi-synthetic beta-lactam antibiotics. This enzyme is mainly produced by bacteria but also by some fungi. In the present study, the filamentous fungus Mucor griseocyanus was used to produce penicillin acylase enzyme (PGA). Its ability to express PGA enzyme in submerged fermentation process was assessed, finding that this fungal strain produces the biocatalyst of interest in an extracellular way at a level of 570 IU/L at 72 h of fermentation; in this case, a saline media using lactose as carbon source and penicillin G as inducer was employed. In addition, a DNA fragment (859 bp) of the pga from a pure Mucor griseocyanus strain was amplified, sequenced, and analyzed in silico. The partial sequence of pga identified in the fungi showed high identity percentage with penicillin G acylase sequences deposited in NCBI through BLAST, especially with the β subunit of PGA from the Alcaligenes faecalis bacterium¸ which is a region involved in the catalytic function of this protein. Besides, the identification of domains in the penicillin G acylase sequence of Mucor griseocyanus showed three conserved regions of this protein. The bioinformatic results support the identity of the gen as penicillin G acylase. This is the first report that involves sequencing and in silico analysis of Mucor griseocyanus strain gene encoding PGA.
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