Immobilization of a Thermostable Diamine Oxidase from Vigna radiate (L.) Wilczek Seedlings

Key Points

• This immobilization significantly improves the thermostability of diamine oxidase, enabling broader applications.
• The enzyme exhibited exceptional performance metrics, maintaining activity at elevated temperatures beyond typical ranges.
• Assessment involved the immobilization of diamine oxidase from Vigna radiate seedlings, focusing on enzyme stability and activity preservation.
• Enhancing the stability of this enzyme may open new possibilities for industrial applications and biochemical processes.