TESTING ENVIRONMENTAL MODULATION OF THE ENZYME CATALASE AS A FRAMEWORK FOR NANO-CATALASE THERAPIES IN OXIDATIVE STRESS-DRIVEN DIABETES

This research paper aims to investigate the activity of the catalase enzyme under varying environmental conditions, including pH value, glucose concentration, and temperature.Catalase is a crucial antioxidant enzyme that breaks down hydrogen peroxide (HO), a highly reactive oxygen species (ROS), into water and oxygen.In diabetic cells, activities like glycation can impair catalase activity.This stimulates how hyperglycemia in diabetes reduces catalase efficiency.We hypothesize that high glucose and extreme pH or temperature will lower enzyme activity and produce less O gas.Our experiment involves Solanum tuberosum (potato) derived catalase extract, observing its reactions with HO and measuring O evolution as an indicator for catalase activity through biological assays under varying environments.The results showed the expected trends: maximum activity at neutral pH and moderate temperature, and reduced activity with high glucose (mimicking diabetic glycation of catalase).Reduced catalase activity in hyperglycemia contributes to ROS buildup.We also discuss nanoparticle-mediated catalase (nano-CAT) delivery, an emerging therapy where catalase is packaged into nanoparticles and sent to target tissues.Polymer nano-capsules carrying catalase have been developed, which help in the decomposition of HO and can protect the cells from oxidative stress.We explore how nano-delivery can enhance enzyme stability and therapeutic efficacy.