Hydrolytic Enzymes in the DNA-Seq Illumina Genome of Aspergillus salvadorensis in the Degradation of Complex Polymers in Tropical Ecosystems (2024-2025)
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Date
2025-04-30
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IKR Journal of Agriculture and Biosciences
Abstract
Bioinformatic analysis of the genome of Aspergillus salvadorensis allowed the identification of an extracellular hydrolase with an unusual structural organization. Unlike typical enzymes, this protein has a segmented arrangement, marked by repetitive sequences (such as AHNTKDSN...), which seem to act as boundaries between different functional domains. This particular architecture suggests an internal specialization that allows it to perform multiple functions within the same molecule. At the protein level, a catalytic triad composed of serine, histidine and aspartate was identified, a distinctive feature of serine hydrolases and glycosyl hydrolases. This configuration favors its activity in slightly acidic conditions, with an optimal pH range between 5.5 and 6.0, which coincides with environments where many fungi usually develop. The protein also has characteristics that ensure its correct functionality outside the cell. A hydrophobic signal peptide at the N-terminal end directs its secretion towards the extracellular medium, while multiple N-glycosylation sites contribute to stabilize its structure, protecting it against adverse conditions such as high temperatures or the action of other degradative enzymes. The degradation of biomass, this enzyme stands out for its functional versatility. The presence of metal-binding domains and motifs associated with antibiotic resistance indicates that it is a protein with multiple functions. Some of its segments are involved in the degradation of polymers for nutrients, while others could act as beta-lactamases, helping to neutralize antimicrobial compounds produced by competing organisms. Indications of chitinase activity are also observed, suggesting a possible role in the degradation of external fungal structures. This functional repertoire is complemented by the presence of other associated enzymes, such as serine proteases involved in obtaining nitrogen, phosphatases related to energy production under limiting conditions and nucleases that contribute to the maintenance of genetic integrity. Overall, this enzyme system reflects a highly efficient adaptive strategy, which allows the organism not only to nourish itself, but also to defend itself and modify its environment. This remarkable metabolic plasticity facilitates its colonization of different ecological niches and, at the same time, opens up interesting possibilities for its application in bioremediation processes and in the development of biotechnological tools.
Keywords: Hydrolases, ORFinder, Aspergillus salvadorensis.
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Keywords
Hydrolases, ORFinder, Aspergillus salvadorensis