Rapid and Simple Purification of Lysozyme from the Egg Shell Membrane
| Autor: | Miyuki Kozuka, Tsutomu Inoue, Takuya Yamane, Iwao Ohkubo, Hiroyoshi Ariga, Sato Murao |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Egg protein
Medicine (miscellaneous) Peptidoglycan Bacterial cell structure Egg Shell chemistry.chemical_compound Egg White Animals Food Industry lysozyme chemistry.chemical_classification Nutrition and Dietetics Chromatography rapid and simple purification Hydrogen-Ion Concentration eggshell membrane Anti-Bacterial Agents Kinetics Enzyme chemistry Muramic Acids Muramidase Lysozyme Eggshell membrane Antibacterial activity Egg white |
| Zdroj: | Journal of Nutritional Science and Vitaminology. 61:101-103 |
| ISSN: | 1881-7742 0301-4800 |
| DOI: | 10.3177/jnsv.61.101 |
| Popis: | Lysozyme (EC 3.2.1.17) is a hydrolytic enzyme that cleaves the β-(1, 4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, a major bacterial cell wall polymer. In the food industry, lysozyme is used as an additive mainly in the production of wine and beer. Lysozyme was found to be localized in the egg shell membrane. In this study, we found that lysozyme was easily purified from the egg shell membrane and that the enzyme also had an antibacterial activity. Furthermore, we found that the antibacterial activity of purified lysozyme from the egg shell membrane was lower than that of purified lysozyme from the egg white at alkaline pH. The method for rapid purification of lysozyme developed in this study should contribute to food industry. |
| Databáze: | OpenAIRE |
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