Lactoperoxidase immobilization on silver nanoparticles enhances its antimicrobial activity

Area of Science:

• Biotechnology
• Materials Science
• Food Science

Background:

• Lactoperoxidase (LPO) is a key antimicrobial protein in milk, vital for natural defense.
• LPO's antimicrobial properties are utilized to extend the shelf life of dairy products.
• Enhancing LPO's stability and efficacy is crucial for industrial applications.

Purpose of the Study:

• To immobilize LPO onto silver nanoparticles (AgNPs) to create an LPO/AgNP conjugate.
• To characterize the synthesized LPO/AgNP conjugate using biophysical techniques.
• To evaluate the enhanced antibacterial activity of the LPO/AgNP conjugate against E. coli.

Main Methods:

• Synthesis and characterization of spherical silver nanoparticles (AgNPs).
• Immobilization of LPO onto AgNPs to form the LPO/AgNP conjugate.
• Assessment of antibacterial activity against E. coli over 10 hours at 2-hour intervals.

Main Results:

• Successful synthesis of spherical AgNPs.
• LPO was effectively immobilized on AgNPs, forming conjugates with average agglomerate sizes of approximately 50 nm.
• The LPO/AgNP conjugate exhibited significantly enhanced antibacterial activity against E. coli compared to free LPO.

Conclusions:

• The immobilization of LPO on AgNPs successfully enhances its antibacterial efficacy.
• This LPO/AgNP conjugate represents a promising advancement for the lactoperoxidase system.
• Potential for improved stability and antimicrobial function in dairy and other industries.