Kinetic studies of cow milk lactoperoxidase
Keywords:
lactoperoxidase, milk whey, substrate specificity, the Michaelis constant, the catalytic constantAbstract
The kinetic parameters of oxidation of natural substrates of lactoperoxidase of cow’s milk whey were obtained. The correlation between the initial substrate oxidation velocity and pH and enzyme concentration were characterized and kinetic parameters of cow milk lactoperoxidase were determined. Cow’s milk lactoperoxidase is characterized by similar optimum pH and kinetic parameters with regard to the oxidation of natural substrates by other peroxidases. The substrate specificity data analysis indicated that the most prefered substrate of cow’s milk lactoperoxidase is SCN–. The results can be used for comparative analysis of lactoperoxidase kinetic properties of different animal species, as well as for quality control in the manufacture of lactoperoxidase-containing foods and cosmetics.
References
- Kussendrager K. D., Van Hooijdonk A. C. Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. B. J. Nutr. 2000. Vol. 84, suppl. 1. P. 19 –25.
- De Wit J. N., Van Hooydonk A. C. M. Structure, functions and applications of lactoperoxidase in natural antimicrobial systems. Neth. Milk Dairy J. 1996. Vol. 50. P. 227–244.
- Thomas E. L., Milligan T. W., Joyner R. E., et al. Antibacterial activity of hydrogen peroxide and the lactoperoxidase-hydrogen peroxide-thiocyanate system against oral streptococci. Infect. Immun. 1994. Vol. 62, issue 2. P. 529 –535.
- Wolfson L. M., Sumner S. S. Antibacterial activity of the lactoperoxidase system : a review. J. Food Prot. 1993. Vol. 56, No. 10. P. 887–892. DOI: 10.4315/0362-028X-56.10.887.
- Ciaccio C., Cambacurta A., De Sanctis G., et al. rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization. Biochem. J. 2006. Vol. 395, part 2. P. 295–301. DOI: 10.1042/BJ20051385.
- Mazumdai A., Chatterjee R., Adak S., et al. Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor. Biochem. J. 1996. Vol. 314. P. 413– 419.
- Kakhanouskaya K. Y., Semak I. V. Kinetic studies of goat milk lactoperoxidase. Proc. Natl. Acad. Sci. Belarus. Biol. ser. 2015. No. 2. P. 83– 87 (in Russ.).
Downloads
Published
Issue
Section
License
The authors who are published in this journal agree to the following:
- The authors retain copyright on the work and provide the journal with the right of first publication of the work on condition of license Creative Commons Attribution-NonCommercial. 4.0 International (CC BY-NC 4.0).
- The authors retain the right to enter into certain contractual agreements relating to the non-exclusive distribution of the published version of the work (e.g. post it on the institutional repository, publication in the book), with the reference to its original publication in this journal.
- The authors have the right to post their work on the Internet (e.g. on the institutional store or personal website) prior to and during the review process, conducted by the journal, as this may lead to a productive discussion and a large number of references to this work. (See The Effect of Open Access.)
