Lysozymes (EC. 126.96.36.199) are widely recognized for their contribution to the antibacterial defense in many animals and their use as a preservative in foods and pharmaceuticals.  The key characteristic for all lysozymes is their ability to hydrolyze the ß-(1-4)-glycosidic bond between the alternating residues of peptidoglycan, a unique bacterial cell wall polymer. There are many approaches to study the lysozyme activity such as using chitooligosaccharides, but these approaches often require study for overall kinetic rates to later dissect into individual rates. Ogata, et. al. were able to create a novel analytical procedure for studying lysozyme activity undergoing a single cleavage reaction, which simplifies the kinetic measurements.
The research group was able to synthesize ß-D-galactosyl-
Ogata, et. al. used quantitative HPLC-UV to aid this development of this novel analytical procedure. They used HPLC-UV to study the enzymatic-transglycosylation reaction for the synthesis of Gal(
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- Tamo Fukamizo, Takeya Minematsu, Yugi Yanase, Katsuya Hayashi, Sachio Goto, Substrate size dependence of lysozyme-catalyzed reaction, Archives of Biochemistry and Biophysics, Volume 250, Issue 2, 1986, Pages 312-321, ISSN 0003-9861, https://doi.org/10.1016/0003-9861(86)90732-0.
- Makoto Ogata, Megumi Matsui, Haruka Kono, Yuka Matsuzaki, Yuna Kato, Taichi Usui, A novel analytical procedure for assaying lysozyme activity using an end-blocked
chitotetraosederivative as substrate, Analytical Biochemistry, Volume 538, 2017, Pages 64-70, ISSN 0003-2697, https://doi.org/10.1016/j.ab.2017.09.015.