Molecular Characterisation of Fungal L-Arginase: A Comparative Study with Therapeutic Implications

By : Akanksha Khare , Richa Jain

Page No: 75-86

Abstract:
L-Arginase (EC 3.5.3.1) is a ureohydrolase enzyme that catalyzes the hydrolysis of L-arginine into L-ornithine and urea. L-Ornithine serves as a precursor for the biosynthesis of polyamines and proline. L-Arginase has been extensively studied for its role in the production of L-ornithine. The goal of this project is to perform a comparative characterisation of L-arginase enzymes derived from various fungal strains, evaluating their enzymatic properties, and their potential therapeutic applications. Fungal isolates were obtained from diverse environmental soil samples. The Fungal strains were screened for their ability to produce L-arginase, and the most potent producers were subjected to detailed enzymatic assays. L-Arginase activity and its efficiency in converting L-arginine into L-ornithine were evaluated using the ninhydrin assay. A temperature (37°C) and a pH of 7.4 were used to mimic in-vivo conditions. 18S rRNA Sequencing was used to confirm the classification. The study identified several fungal isolates exhibiting high L-arginase production and robust enzymatic activity at physiological pH, particularly isolates exhibiting high enzyme activity under physiological conditions (pH 7.4). The results suggest that fungal L-arginase could be a viable candidate for industrial-scale production of L-ornithine for use in targeted therapies certainly related to cancer. Enzyme activity and stability were strongly influenced by optimised culture and reaction conditions. The findings highlight the importance of optimising enzyme production for industrial applications. The report lays the foundation for future investigations into the genetic and metabolic pathways underlying high-yield L-arginase production in fungi, paving the way for more sustainable and cost-effective biotechnological approaches in cancer therapy.

Authors
Akanksha Khare : CSRD, People’s University, Bhopal, Madhya Pradesh,
Richa Jain: CSRD, People’s University, Bhopal, Madhya Pradesh,
 

DOI: https://doi.org/10.32381/JPSR.2026.42.01.8