Study On Antimicrobial Peptides Teleased By Enzymatic Hydrolysis Of Lysozyme

Lysozyme is also called N-acetyl murein hydrolase is devoted to chitosan, effectsof bio self generated glycoside hydrolase in some objective microbial cell wall, is anatural, non-toxic, high security protease, is widely used in industry, pharmaceutical,biological research. With the in-depth study of lysozyme, we found that lysozyme is anon broad-spectrum antimicrobial agent, its inhibitory effect on Gram positive bacteriais stronger, and bacteriostatic action on Gram negative bacteria is weaker, and thescientific research on a series of improved antibacterial spectrum of lysozyme.Modifiedlysozyme antimicrobial spectrum can be divided into4main types: physical methods,chemical methods and genetic fusion method, hydrolysis method, this experimentadopts hydrolysis method improved the antibacterial spectrum of lysozyme.The main material experiment is egg white lysozyme, pepsin and trypsin. Theeffect of lysozyme by pepsin and trypsin, the products at different stages of reaction fordetermination of enzyme activity, and through the electrophoresis results determinedcompletely by the enzyme lysozyme into polypeptide. The polypeptide productpurification, determination of polypeptide products on bacterial bacteriostasispurification method of bacteriostatic circle, and determination of polypeptide productson pH and thermal stability.The experimental results show that, by pepsin and trypsin lysozyme to generate thepeptide products, enhance the determination of enzyme inhibition zone methodhydrolysates on Gram negative bacteria inhibitory ability. The enzyme was divided intopeptide, the peptide products with strong antibacterial activity, antibacterial spectrum oflysozyme can effectively expand. Determination of the activity of lysozyme in solutionafter, the associated activity and solution temperature, solution are compared, results in90℃activity generally lower than25℃. In addition, polypeptide products lose activityat25℃and90℃, but it on Gram negative bacteria have antibacterial activity, enzymeactivity and antibacterial capability that is not directly proportional to. Bacteriostaticability of product and lysozyme pH, different temperature conditions of enzymolysiswere determined and compared, with the increase in temperature and pH, antimicrobialactivity of lysozyme decreased greatly, and the hydrolysis product of antibacterial ability but only minor changes, proof of enzymatic hydrolysates on pH and thermalstability of strong.The experiment improved the antimicrobial spectrum of lysozyme, and the productof pH and thermal stability is far better than the lysozyme. The product obtained byenzymolysis polypeptide on the outside of the lower requirements, and also has anatural non-toxic, good stability characteristics, more suitable for widely put into actualproduction in our life.