Naringinase: A comprehensive review on its characteristics, production, and biotechnological applications

Naringinase is a bifunctional enzyme exhibiting both α-L-rhamnosidase and β-D-glucosidase activity, primarily utilized for the hydrolysis of bitter compounds like naringin in citrus products. This enzymatic action yields naringenin, a bioactive flavonoid known for its significant antioxidant, anti-inflammatory, and cardioprotective properties. Given its dual enzymatic function and substrate specificity, naringinase has garnered substantial interest across the food, pharmaceutical, and broader biotechnological sectors. This comprehensive review critically examines recent advancements concerning naringinase, focusing on its microbial production, optimization strategies in fermentation, purification methods, and various immobilization technologies. Aspergillus niger and Penicillium decumbens are identified as the predominant microbial sources for naringinase production, with solid-state fermentation demonstrating economic and cost-effectiveness over submerged fermentation. The application of diverse immobilization techniques, including adsorption, covalent binding, and encapsulation, has been shown to significantly enhance the enzyme's catalytic stability, reusability, and overall efficiency in applications such as juice debittering and the development of functional foods. While advanced biocatalysis approaches like recombinant expression and enzyme engineering offer promising improvements in catalytic properties, the persistent challenges related to production scalability and purification costs warrant further assessment. The integration of sustainable solid-state fermentation with cutting-edge nanomaterials holds considerable promise, opening new avenues for naringinase applications in environmental biotechnology and personalized medicine.