A comparative analysis of catalase activity in animal and plant tissues collected in Pineville, Rapid Parish, Louisiana, USA

Catalase (EC 1.11.1.6) is a ubiquitous enzyme that catalyzes the disproportionation of hydrogen peroxide (H2O2) into water and oxygen. This study investigated catalase activity in five distinct biological samples: chicken liver, beef muscle, potato tuber, carrot root, and banana pulp. Crude enzyme extracts were prepared from each tissue, and their activity was assessed by measuring the foam height generated upon the addition of a 3% H2O2 solution. The objective was to compare catalase activity across diverse animal and plant tissues, reflecting their varying metabolic demands and roles in oxidative stress management. As hypothesized, chicken liver extract exhibited the highest catalase activity, producing the most vigorous effervescence and greatest foam height (approximately 5–6 cm). Beef muscle demonstrated substantial activity (approximately 3 cm), albeit lower than liver. Potato and banana extracts showed moderate activity (approximately 1.5–2.0 cm), while carrot root extract exhibited minimal activity (<0.5 cm). These findings are consistent with established knowledge regarding catalase distribution, where highly metabolically active and detoxifying organs like the liver contain abundant catalase, and certain plant tissues demonstrate differential levels. The experiment successfully demonstrated that catalase activity varies significantly among different biological tissues, correlating with their specific physiological functions and exposure to reactive oxygen species.