Category
Basic
Description
This study investigates how replacing the native iron heme with manganese or cobalt protoporphyrins affects the enzymatic activity of horseradish (HRP), pumpkin skin (PKS), and butternut squash (BNT) peroxidases. A heme extraction protocol was adapted for generating apoenzymes by removing the native iron heme cofactor, and extraction was confirmed using UV-vis spectroscopy. While initial reconstitution of apo-HRP with manganese protoporphyrin IX appeared to be incomplete based on UV-vis analysis, the results suggested that manganese incorporation modifies the spectroscopic characteristics of the native enzyme. Comparing horseradish, pumpkin skin, and butternut peroxidases will reveal potential differences in metal-dependent activity and stability among plant sources. This, in turn, will potentially inform the design of engineered enzymes with improved efficiency and stability for biotechnological applications.
Investigating the Role of the Active-Site Metal in Plant Peroxidase Catalysis
Basic
This study investigates how replacing the native iron heme with manganese or cobalt protoporphyrins affects the enzymatic activity of horseradish (HRP), pumpkin skin (PKS), and butternut squash (BNT) peroxidases. A heme extraction protocol was adapted for generating apoenzymes by removing the native iron heme cofactor, and extraction was confirmed using UV-vis spectroscopy. While initial reconstitution of apo-HRP with manganese protoporphyrin IX appeared to be incomplete based on UV-vis analysis, the results suggested that manganese incorporation modifies the spectroscopic characteristics of the native enzyme. Comparing horseradish, pumpkin skin, and butternut peroxidases will reveal potential differences in metal-dependent activity and stability among plant sources. This, in turn, will potentially inform the design of engineered enzymes with improved efficiency and stability for biotechnological applications.
