Pathogenic and Industrial Implications of Lipase Enzyme Extracted from Aspergillus niger: A Comparative Study of Biotechnological Applications and Clinical Risks
Aspergillus niger is a widely distributed filamentous fungus known for its significant role in industrial biotechnology and its potential as an opportunistic pathogen. This study investigated the production, characterization, and industrial applications of A. niger-derived lipase while assessing its pathogenic risks and biosafety concerns. Lipase production was optimized using solid-state fermentation (SSF) and submerged fermentation (SmF) techniques, with results indicating maximum enzyme activity at pH 7.5 and 40°C. The enzyme demonstrated strong substrate specificity, particularly for long-chain triglycerides, making it highly suitable for detergents, pharmaceuticals, and food industries. Comparative analysis with bacterial and yeast-derived lipases revealed that A. niger lipase offers high substrate specificity and cost-effective production, but has moderate thermostability compared to bacterial lipases. The study also reviewed clinical cases of A. niger-related infections, particularly otomycosis, onychomycosis, and pulmonary aspergillosis, highlighting its impact on immunocompromised individuals. Antifungal resistance patterns and biosafety concerns, particularly mycotoxin contamination, were assessed, emphasizing the need for regulatory measures in large-scale enzyme production. Despite its pathogenic potential, GRAS-certified A. niger strains remain a reliable source of industrial enzymes, provided that strict quality control and safety protocols are followed. This research contributes to the ongoing biotechnological advancements in enzyme production while addressing the clinical and regulatory challenges associated with A. niger. Future studies should focus on genetic modifications, enzyme immobilization techniques, and sustainable fermentation strategies to enhance the stability, efficiency, and biosafety of A. niger-derived lipases.
Authors
- Sumera Sajjad (ORCID: https://orcid.org/0000-0001-6982-5965)
- Indrasish Ray Chaudhuri
- Arshad Nawaz Chaudhry
- Qurat Ul Ain (ORCID: https://orcid.org/0000-0003-4092-6900)
- Ramisha Kamran
Publication Details
- Journal
- Falcons Journal of Advanced Research
- Published
- 2025-01-01
- DOI
- https://doi.org/10.63287/609256
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 0.00