ArticleMolecules (Basel, Switzerland)2022
Study on Antibacterial Activity and Structure of Chemically Modified Lysozyme.
Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Effects of ultrasound-heat pretreated egg white powder addition on the quality, gel properties, and metatranscriptomic profiles of yogurt.Food chemistry: X · 2026Article
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- Photocatalysis and Photodynamic Therapy in Diabetic Foot Ulcers (DFUs) Care: A Novel Approach to Infection Control and Tissue Regeneration.Molecules (Basel, Switzerland) · 2025Review
- Enhanced Antibacterial Activity of Hydrophobic Modified Lysozyme Against Gram-Negative Bacteria Without Accumulated Resistance.Molecules (Basel, Switzerland) · 2025Article
- Evaluation of Quinazolin-2,4-Dione Derivatives as Promising Antibacterial Agents: Synthesis, In Vitro, In Silico ADMET and Molecular Docking Approaches.Molecules (Basel, Switzerland) · 2024Article
- Ascaridia galli, a common nematode in semiscavenging indigenous chickens in Bangladesh: epidemiology, genetic diversity, pathobiology, ex vivo culture, and anthelmintic efficacy.Poultry science · 2024Article
- Cyclization of Chalcone Derivatives: Design, Synthesis,ACS omega · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysozyme is a natural protein with a good bacteriostatic effect, but its poor inhibition of Gram-negative bacteria limits its development potential as a natural preservative. Therefore, the modification of natural lysozyme to expand the antimicrobial spectrum become the focus of lysozyme study. Egg white lysozyme has low cost, rich content in nature, is easy to obtain, strong stability, and high enzyme activity, so it can be applied in the modification of lysozyme. Egg white lysozyme was modified by chemical methods using organic acids. Caffeic acid and p-coumaric acid in organic acids were used as modifiers, and 1-Ethyl-3- (3-dimethylaminopropyl) carbodiimide hydrochloride and N-hydroxy succinimide were used as dehydration condensation agents during modification. A certain degree of modified lysozyme was obtained through appropriate modification conditions. The antibacterial properties and structure of the obtained two organic acid-modified lysozymes were compared with natural enzymes. The results showed that compared with the native enzyme, the activity of modified lysozyme decreased, but the inhibitory effect on Gram-negative bacteria was enhanced. The minimum inhibitory concentrations of caffeic acid-modified enzyme and p-coumaric acid-modified enzyme on
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