Potent Antibacterial Peptides from Enzymatically Hydrolyzed Hen Egg White Lysozyme | ||||
Benha Veterinary Medical Journal | ||||
Article 14, Volume 35, Issue 2, December 2018, Page 150-156 PDF (962.34 K) | ||||
Document Type: Original Article | ||||
DOI: 10.21608/bvmj.2018.96127 | ||||
View on SCiNiTO | ||||
Authors | ||||
Dina, A. Awad1; Hamdi, A. Mohammed1; Adham, M. Abdou1; Sobhy, A. El Sohaimy2 | ||||
1Department of Food Hygiene, Faculty of Veterinary Medicine, Benha University, Egypt. | ||||
2Food Technology ARID Land Research Institute, City of Scientific Research and Technology Application- Borg Elarb-Alexanderia. | ||||
Abstract | ||||
Egg white is considered as a rich source of high quality proteins with various bioactive peptides. It considers the richest source of lysozyme which is a bacteriolytic enzyme. Our target was to produce potent peptides with cheap and simple method from lysozyme as a natural food preservative for further application in food. Lysozyme is mostly active against Gram positive bacteria than Gram negative bacteria. Various strategies have been used to increase antimicrobial activity of lysozyme against Gram-negative bacteria. Enzymatic hydrolysis of proteins can be used to release bioactive fractions using different enzymes to release bioactive fractions. Due to increasing demand for natural food preservatives, lysozyme has become increasingly important in food processing. Therefore, there is a need to develop an efficient and simple methodology for increasing its activity. So this research study the activity of lysozyme hydrolysates under different pH values using pepsin then determine the antibacterial using liquid broth method and determine the lytic activity. We found that lysozyme hydrolysates under pH 3.0 LzP3 gave the most antibacterial active peptide against Gram negative bacteria with more potency against Gram positive bacteria. On conclusion LzP3 contains bioactive peptides that can be applied for safety food biopreservation. | ||||
Keywords | ||||
Lysozyme; peptic hydrolysis; lytic activity; antibacterial activity | ||||
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