Laktoperoksidaz enzimini inhibe eden maddelerin belirlenmesi için yapılan bazı çalışmaların incelenmesi ve enzimin uygulama alanlarının örneklendirilmesi

Lactoperoxidase (LPO; E.C. 1.11.1.7) was isolated from milk in 1940s by Theorell et al., and in the following years, it was purified by Morrison et al. using ion-exchange chromatography. This enzyme is a glycoprotein that is a member of the peroxidase family and contains the heme group as a prosthetic group. Lactoperoxidase is an oxidoreductase enzyme that exhibits antimicrobial action against pathogens secreted from the digestive tract of newborns. This enzyme is found in saliva and tears as well as in milk. The determination of lactoperoxidase inhibitors and how the enzyme will be affected in case of antibiotic use is very important for newborn health. The studies reviewed here contain references for the determination of the inhibitors of lactoperoxidase and the degree of inhibition of these inhibitors, and the use of antibiotics in newborns. At the same time, it is very important to know the substances that increase the activity of the enzyme, especially for use in the food and pharmaceutical industries.

___

  • 1. AEHLE, W., 2004. Enzymes in Industry Production and Application. Wiley-VCH Verlag, Weinheim, p.484.2. Berg, Jeremy M., John L. Tymoczko, and Lubert Stryer. BIOCHEMISTRY. 6th ed. New York: W. H. FREEMAN AND COMPANY, 2007.3. Berg J., Tymoczko J. and Stryer L. (2002) Biochemistry. W. H. Freeman and Company ISBN 0-7167-4955-64. Çankaya, M., Şişecioğlu, M., Yörük, Ö., Özdemir, H., ‘‘In Vitro Effects of Some Antibiotic Drugs on Bovine Lactoperoxidase Enzyme’’ Turkish Journal of Medical Sciences, 36, 301-306, (2006)5. Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 ed.). Wiley-Interscience. ISBN 0471205036.6. Hussain S, Slikker W, Ali SF. Age related changes in antioxidant enzymes, superoxide dismutase, catalase, glutathione peroxidase and glutathione in different region of mouse brain. International Journal of Developmental Neuroscience 1995;13:811–817. DOI: 10.1016/07365748(95)00071-27. Kumar R, Bhatla KL. Purification, crystallization and preliminary x-ray crystallographic analysis of lactoperoxidase from buffalo milk. Acta Crystallographica. 1995;51:10948. Kussendrager KD, van Hooijdonk ACM. Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. British Journal of Nutrition. 2000;84:19–25. 10.1017/S00071145000022089. Morrison M, Allen PZ, Bright J, Jayasinghe W. Lactoperoxidase. V. Identification and isolation of lactoperoxidase from salivary gland. Arch Biochem Biophys. 1965;111:126–133. 10. Morrison M, Allen PZ. Lactoperoxidase: identification and isolation from Harderian and lacrimal glands. Science. 1966;152:1626–1628. 11. Morrison M, Hamilton HB, Stotz E. The isolation and purification of lactoperoxidase by ion exchange chromatography. J Biol Chem. 1957;228:767–776. 12. Ozdemir H, Aygul I, Kufrevioğlu OI. Laktoperoksidazın sığır sütününden arıtılması ve kinetik özelliklerinin incelenmesi. Preparatif Biyokimya ve Biyoteknoloji. 2001; 31 : 125-13413. Pourtois M, Binet C, Van Tieghem N, Courtois PR, Vandenabbeele A, Thirty L. Saliva can contribute in quick inhibition of HIV infectivity. AIDS. 1991;5:598–60014. Reiter B, Perraudin JP. Lactoperoxidase: biological functions. In: Peroxydases in Chemistryand Biology. Boca Raton: CRC Press; 1991. 143–180 pp15. Reiter B, HaÈrnulv G. Lactoperoxidase antibacterial system: natural occurrence, biological functions and practical applications. Journal of Food Protection. 1984;47:724–73216. Reiter B (1983). "The biological significance of lactoferrin". Int J Tissue React. 5 (1): 87– 96. 17. Roger V, Tenovuo J, Lenander-Lumikari M, Söderling E, Vilja P (1994). "Lysozyme and lactoperoxidase inhibit the adherence of Streptococcus mutans NCTC 10449 (serotype c) to saliva-treated hydroxyapatite in vitro". Caries Res. 28 (6): 421–8. 18. Sievers G. Structure of milk lactoperoxidase. A study using circular dischroism and difference absorption sperctroscopy. Biochimica et Biophysica Acta. 1980;624: 24919. Singh, A.K., Singh, N., Sharma, S., Kaur, P., Srinivasan, A., Singh, T.P. (September 2007). "Crystal structure of lactoperoxidase at 2.4A resolution". J. Mol. Biol. 376(1): 1060– 1075. 20. SMITH, J.E., 2004. Biotechnology. Cambridge University Press, New York, p.27121. TUNAİL, N., 2009. Mikrobiyoloji. Pelin Ofset, Ankara, s.448.22. Ishfag A. Sheikh, Ghulam Md. Ashraf, Mohammad A. Kamal ve Mohd A. Beg (2018). “Structural studies on inhibitory mechanisms of antibiotic, corticosteroid and catecholamine molecules on lactoperoxidase”. Life Sciences, Volume 207, p.412-41923. Jörg Flemmig, Jürgen Arnhold, Isabell Noetzel,Hans-Wilhelm Rauwald (2015). “,Leonurus cardiaca L. herb extracts and their constituents promote lactoperoxidase activity,”. Journal of Functional Foods, Volume 17, Pages 328-339.24. Sofía Lara-AguilarSamuel D.Alcaine (March 2019). “ Lactose oxidase: A novel activator of the lactoperoxidase system in milk for improved shelf life”. Journal of Dairy Science, Volume 102, Issue 3, Pages 1933-1942.25. Marziyeh BorjianBoroujeni, HashemNayeri (2018). “Stabilization of bovine lactoperoxidase in the presence of ectoine”. Food Chemistry Volume 265, Pages 208-215.26. Mayumi Nakada, Shun'ichi Dosako, RyogoHirano, Minoru Oooka, Ichiro Nakajima (1996). “Lactoperoxidase suppresses acid production in yoghurt during storage under refrigeration”. International Dairy Journal Volume 6, Issue 1, Pages 33-42.27. J.Martı́nez-Gomis, A.Fernández-Solanas, M.Viñas, P.González, M.E.Planas, S.Sáncheza (1999). “ Effects of topical application of free and liposome-encapsulated lactoferrin and lactoperoxidase on oral microbiota and dental caries in rats”. Archives of Oral Biology Volume 44, Issue 11, Pages 901-906.28. Hanna Lee ve Sea C.Min (2013). “ Antimicrobial edible defatted soybean meal-based films incorporating the lactoperoxidase system”. LWT - Food Science and Technology Volume 54, Issue 1, Pages 42-50.29. Mohamed Cissé , Jessica Polidori ,Didier Montet, Gérard Loiseau, Marie Noëlle Ducamp-Collin (2015). “ Preservation of mango quality by using functional chitosan-lactoperoxidase systems coatings”. Postharvest Biology and Technology Volume 101, Pages 10-14.