Lactoperoxidase immobilization on silver nanoparticles enhances its antimicrobial activity

Lactoperoxidase (LPO) is an antimicrobial protein present in milk that plays an important role in natural defence mechanisms during neonatal and adult life. The antimicrobial activity of LPO has been commercially adapted for increasing the shelf life of dairy products. Immobilization of LPO on silve...

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Bibliographic Details
Published in:Journal of dairy research 2018-11, Vol.85 (4), p.460-464
Main Authors: Sheikh, Ishfaq Ahmad, Yasir, Muhammad, Khan, Imran, Khan, Sher Bahadur, Azum, Naveed, Jiffri, Essam Hussain, Kamal, Mohammad Amjad, Ashraf, Ghulam Md, Beg, Mohd Amin
Format: Article
Language:English
Subjects:
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Enzymes, Immobilized - pharmacology
Escherichia coli - drug effects
Lactoperoxidase - chemistry
Lactoperoxidase - metabolism
Lactoperoxidase - pharmacology
Metal Nanoparticles - chemistry
Silver - chemistry
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Summary:Lactoperoxidase (LPO) is an antimicrobial protein present in milk that plays an important role in natural defence mechanisms during neonatal and adult life. The antimicrobial activity of LPO has been commercially adapted for increasing the shelf life of dairy products. Immobilization of LPO on silver nanoparticles (AgNPs) is a promising way to enhance the antimicrobial activity of LPO. In the current study, LPO was immobilized on AgNPs to form LPO/AgNP conjugate. The immobilized LPO/AgNP conjugate was characterized by various biophysical techniques. The enhanced antibacterial activity of the conjugate was tested against E. coli in culture at 2 h intervals for 10 h. The results showed successful synthesis of spherical AgNPs. LPO was immobilized on AgNPs with agglomerate sizes averaging approximately 50 nm. The immobilized conjugate exhibited stronger antibacterial activity against E. coli in comparison to free LPO. This study may help in increasing the efficiency of lactoperoxidase system and will assist in identifying novel avenues to enhance the stability and antimicrobial function of LPO system in dairy and other industries.
ISSN:0022-0299
1469-7629
DOI:10.1017/S0022029918000730