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Inhibition Kinetics of Sesamol Against Lactoperoxidase System

Yıl 2020, Cilt: 9 Sayı: 4, 389 - 395, 02.01.2021
https://doi.org/10.37989/gumussagbil.790529

Öz

Rich in bioactive components such as antioxidant systems, milk is one of the indispensable products of a healthy diet. It has a natural defense system against harmful micro-organisms. This system is especially important for the growth and development periods of babies. Lactoperoxidase (LPO; EC 1.11.1.7), which is in the oxidoreductase enzyme class, is a member of the peroxidase family commonly found in humans and animals. Sesamol, a compound derived from sesame seeds, is a molecule widely studied by the scientists for the treatment of various diseases and disorders. In this study, in vitro inhibition parameters of sesamol on bovine lactoperoxidase system were determined. The LPO enzyme was purified 467.51 fold with a yield of 75.99% in one step with an affinity chromatography technique using sulfanilamide as ligand. It was determined that sesamol inhibits LPO enzyme strongly at nM level. IC50 and Ki values for Sesamol were calculated as 138.629 and 80.599±3.669, respectively. Also, sesamol showed a competitive inhibition effect on LPO.

Kaynakça

  • 1. Sanchez-Sanchez, ML, Garcia-Vigara, A, Hidalgo-Mora, JJ, Garcia-Perez, MA, Tarin, J, Cano, A. (20202). Mediterranean diet and health: A systematic review of epidemiological studies and intervention trials. Maturitas, 136, 25-37.
  • 2. Albonico, F, Barelli, C, Albanese, D, Manica, M, Partel, E, Rosso, F, Ripellino, S, Pindo, M, Donati, C, Zecconi, A, Mortarino, M, Hauffe, HC. (2020). Raw milk and fecal microbiota of commercial Alpine dairy cows varies with herd, fat content and diet. Plos one, 15 (8), e0237262.
  • 3. Mastorakou, D, Ruark, A, Weenen, H, Stahl, B, Stieger, M. (2019). Sensory characteristics of human milk: Association between mothers' diet and milk for bitter taste. Journal of dairy science, 102 (2), 1116-1130.
  • 4. Erdem, HU, Kalın, R, Özdemir, N, Özdemir, H. (2015). Purification and Biochemical Characterization of Peroxidase İsolated From White Cabbage (Brassica oleracea Var. Capitata F. Alba). International Journal of Food Properties, 18, 2099-2109.
  • 5. Somturk, B, Kalin, R, Özdemir, N. (2014). Purification of Peroxidase From Red Cabbage (Brassica oleracea Var. Capitata F. Rubra) by Affinity Chromatography. Applied Biochemistry and Biotechnology, 173, 1815-1828.
  • 6. Halliwell, B. (1984). Oxygen radicals: A Commonsense Look at Their Nature and Medical Importance. Medical Biology, 62, 71-77.
  • 7. Kumar, R, Bhatla, KL. (1995). Purification, Crystallization and Preliminary X-Ray Crystallographic Analysis of Lactoperoxidase from Buffalo Milk. Acta Crystallographica, 51, 1094-1096.
  • 8. Fonteh, FA, Grandison, AS, Lewis, MJ. (2002). Variations of Lactoperoxidase Activity and Thiocyanate Content in Cows' and Goats' Milk Throughout Lactation. Journal of Dairy Research. 69, 401-409.
  • 9. El Agamy, EI, Ruppanner, R, Ismail, A, Champagne, CP, Assaf, R. (1992). Antibacterial and Antiviral Activity of Camel Milk Protective Proteins. Journal of Dairy Research, 59 (2), 169-175.
  • 10. Köksal, Z, Kalın, R, Gülçin, İ, Özdemir, H, Atasever, A. (2016). The Impact of Some Avermectins on Lactoperoxidase in Bovine Milk. International Journal of Food Properties, 19 (6), 1207-1216.
  • 11. Shyu, YS, Hwang, LS. (2002). Antioxidative Activity of the Crude Extract of Lignan Glycosides from Unroasted Burma Black Sesame Meal. Food Research International, 35, 357-365.
  • 12. Bankole, MA, Shittu, LAJ, Ahmed, TA, Bankole, MN, Shittu, RK, Terkula, K, Ashiru, OA. (2007). Synergistic Antimicrobial Activities of Phytoestrogens in Crude Extracts of Two Sesame Species against Some Common Pathogenic Microorganisms. African Journal of Traditional, Complementary and Alternative Medicines, 4, 427-433.
  • 13. Alencar, JS, Pietri, S, Culcasi, M, Orneto, C, Piccerelle, P, Reynier, JP, Portugal, H, Nicolay, A, Kaloustian, J. (2009). Interactions and Antioxidant Stability of Sesamol in Dry-emulsions. Journal of Thermal Analysis and Calorimetry, 98, 133-143.
  • 14. Shindler, JS, Bardsley, W. (1975). Steady-State Kinetics of Lactoperoxidase With ABTS as Chromogens. Biochemical and Biophysical Research Communications, 67, 1307-1312.
  • 15. Bradford, MM. (1976). A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding. Analytical Biochemistry, 72 (1-2), 248-251.
  • 16. Köksal, Z, Kalın, R, Gerni, S, Gülçin, İ, Özdemir, H. (2017). The Inhibition Effects of Some Natural Products on Lactoperoxidase Purified from Bovine Milk. Journal of Biochemical and Molecular Toxicology, 31 (9), E21939.
  • 17. Laemmli, DK. (1970). Clevage of Structual Proteins During in Assembly of the Head of Bacteriophage T4. Nature, 227, 680-683.
  • 18. Madureira, AR, Pereira, CI, Gomes, AMP, Pintado, ME, Malcata, FX. (2007). Bovine Whey Proteins - Overview on Their Main Biological Properties. Food Research International, 40, 1197-1211.
  • 19. López-Expósito, I, Manso, MA, López-Fandiño, R, Recio, I. (2008). Activity Against Listeria Monocytogenes of Human Milk During Lactation. A Preliminary Study. Journal of Dairy Research, 7 (1), 24-29.
  • 20. Sarıkaya, SBO, Şişecioğlu, M, Çankaya, M, Gülçin, İ, Ozdemir, H. (2015). Inhibition Profile of A Series of Phenolic Acids on Bovine Lactoperoxidase Enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 30(3), 479-483.
  • 21. Şişecioğlu, M, Uğuz, MT, Çankaya, M, Özdemir, H, Gülçin, İ. (2011). Effects of Ceftazidime Pentahydrate, Prednisolone, Amikacin Sulfate, Ceftriaxone Sodium and Teicoplanin on Bovine Milk Lactoperoxidase Activity. Internatıonal Journal of Pharmacology, 7, 79-83.
  • 22. Shah, A, Lobo, R, Krishnadas, N, Surubhotla, R. (2019). Sesamol and Health-A Comprehensive Review. Indian Journal of Pharmaceutical Education and Research, 53 (2), 28-42.
  • 23. Atmaca,, U, Yıldırım A, Taslimi, P, Tuncel, Çelik S, Gülçin, İ, Supuran,, CT, Çelik, M. (2018). Intermolecular Amination of Allylic and Benzylic Alcohols Leads to Effective Inhibitions of Acetylcholinesterase Enzyme and Carbonic Anhydrase I and II Isoenzymes. Journal of Biochemical and Molecular Toxicology, 32, e22173.
  • 24. Jan, KC, Ho, CT, Hwang, LS. (2008). Bioavailability and Tissue Distribution of Sesamol in Rat. Journal of Agricultural and Food Chemistry, 56, 7032-7037.
  • 25. Bayrak, Ç, Taslimi,, P, Kahraman, HS, Gülçin, İ, Menzek, A. (2019). The First Synthesis, Carbonic Anhydrase Inhibition and Anticholinergic Activities of Some Bromophenol Derivatives with Including Natural Products. Bioorganic Chemistry, 85, 128-139.
  • 26. Topal, M. (2019). The Inhibition Profile of Sesamol Against Α-Glycosidase and Acetylcholinesterase Enzymes. International Journal of Food Properties, 22 (1), 1527-1535.
  • 27. Özyürek, IN, Kalın, R, Özdemir, H. (2020). The Inhibition Effects of D-Penicillamine, D-Penicillamine disulfide and N-Acetyl-D-Penicillamine on Lactoperoxidase Enzyme Activity. Journal of the Institute of Science and Technology, 10 (2), 1146-1153.

Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği

Yıl 2020, Cilt: 9 Sayı: 4, 389 - 395, 02.01.2021
https://doi.org/10.37989/gumussagbil.790529

Öz

Antioksidan sistemleri gibi biyoaktif bileşenlerce zengin olan süt, sağlıklı bir beslenmenin vazgeçilmez ürünlerinden bir tanesidir. Süt, zararlı mikro-organizmalara karşı doğal bir savunma sistemine sahiptir. Bu sistem, özellikle bebeklerin büyüme ve gelişme dönemleri için çok önemlidir. Oksidoredüktaz enzim sınıfında olan laktoperoksidaz (LPO; EC 1.11.1.7), doğada yaygın olarak insanlarda ve hayvanlarda bulunan peroksidaz ailesinin bir üyesidir. Susam tohumlarından elde edilen bir bileşik olan sesamol, çeşitli hastalık ve bozuklukların tedavisi için bilim camiası tarafından geniş çapta çalışılmış bir moleküldür. Bu çalışmada, sığır laktoperoksidaz sistemi üzerine sesamolün in vitro inhibisyon parametreleri belirlenmiştir. LPO enzimi, ligant olarak sülfanilamitin kullanıldığı bir afinite kromatografisi tekniği ile tek kademede %75,99 verim ile 467,51 kat saflaştırıldı. Sesamol LPO enzimini nM’lar seviyede güçlü bir şekilde inhibe ettiği belirlendi. Sesamol için IC50 ve Ki değerleri sırasıyla 138,629 ve 80,599±3,669 olarak hesaplandı. Aynı zamanda sesamol LPO üzerine yarışmalı bir inhibisyon etkisi gösterdi.

Kaynakça

  • 1. Sanchez-Sanchez, ML, Garcia-Vigara, A, Hidalgo-Mora, JJ, Garcia-Perez, MA, Tarin, J, Cano, A. (20202). Mediterranean diet and health: A systematic review of epidemiological studies and intervention trials. Maturitas, 136, 25-37.
  • 2. Albonico, F, Barelli, C, Albanese, D, Manica, M, Partel, E, Rosso, F, Ripellino, S, Pindo, M, Donati, C, Zecconi, A, Mortarino, M, Hauffe, HC. (2020). Raw milk and fecal microbiota of commercial Alpine dairy cows varies with herd, fat content and diet. Plos one, 15 (8), e0237262.
  • 3. Mastorakou, D, Ruark, A, Weenen, H, Stahl, B, Stieger, M. (2019). Sensory characteristics of human milk: Association between mothers' diet and milk for bitter taste. Journal of dairy science, 102 (2), 1116-1130.
  • 4. Erdem, HU, Kalın, R, Özdemir, N, Özdemir, H. (2015). Purification and Biochemical Characterization of Peroxidase İsolated From White Cabbage (Brassica oleracea Var. Capitata F. Alba). International Journal of Food Properties, 18, 2099-2109.
  • 5. Somturk, B, Kalin, R, Özdemir, N. (2014). Purification of Peroxidase From Red Cabbage (Brassica oleracea Var. Capitata F. Rubra) by Affinity Chromatography. Applied Biochemistry and Biotechnology, 173, 1815-1828.
  • 6. Halliwell, B. (1984). Oxygen radicals: A Commonsense Look at Their Nature and Medical Importance. Medical Biology, 62, 71-77.
  • 7. Kumar, R, Bhatla, KL. (1995). Purification, Crystallization and Preliminary X-Ray Crystallographic Analysis of Lactoperoxidase from Buffalo Milk. Acta Crystallographica, 51, 1094-1096.
  • 8. Fonteh, FA, Grandison, AS, Lewis, MJ. (2002). Variations of Lactoperoxidase Activity and Thiocyanate Content in Cows' and Goats' Milk Throughout Lactation. Journal of Dairy Research. 69, 401-409.
  • 9. El Agamy, EI, Ruppanner, R, Ismail, A, Champagne, CP, Assaf, R. (1992). Antibacterial and Antiviral Activity of Camel Milk Protective Proteins. Journal of Dairy Research, 59 (2), 169-175.
  • 10. Köksal, Z, Kalın, R, Gülçin, İ, Özdemir, H, Atasever, A. (2016). The Impact of Some Avermectins on Lactoperoxidase in Bovine Milk. International Journal of Food Properties, 19 (6), 1207-1216.
  • 11. Shyu, YS, Hwang, LS. (2002). Antioxidative Activity of the Crude Extract of Lignan Glycosides from Unroasted Burma Black Sesame Meal. Food Research International, 35, 357-365.
  • 12. Bankole, MA, Shittu, LAJ, Ahmed, TA, Bankole, MN, Shittu, RK, Terkula, K, Ashiru, OA. (2007). Synergistic Antimicrobial Activities of Phytoestrogens in Crude Extracts of Two Sesame Species against Some Common Pathogenic Microorganisms. African Journal of Traditional, Complementary and Alternative Medicines, 4, 427-433.
  • 13. Alencar, JS, Pietri, S, Culcasi, M, Orneto, C, Piccerelle, P, Reynier, JP, Portugal, H, Nicolay, A, Kaloustian, J. (2009). Interactions and Antioxidant Stability of Sesamol in Dry-emulsions. Journal of Thermal Analysis and Calorimetry, 98, 133-143.
  • 14. Shindler, JS, Bardsley, W. (1975). Steady-State Kinetics of Lactoperoxidase With ABTS as Chromogens. Biochemical and Biophysical Research Communications, 67, 1307-1312.
  • 15. Bradford, MM. (1976). A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding. Analytical Biochemistry, 72 (1-2), 248-251.
  • 16. Köksal, Z, Kalın, R, Gerni, S, Gülçin, İ, Özdemir, H. (2017). The Inhibition Effects of Some Natural Products on Lactoperoxidase Purified from Bovine Milk. Journal of Biochemical and Molecular Toxicology, 31 (9), E21939.
  • 17. Laemmli, DK. (1970). Clevage of Structual Proteins During in Assembly of the Head of Bacteriophage T4. Nature, 227, 680-683.
  • 18. Madureira, AR, Pereira, CI, Gomes, AMP, Pintado, ME, Malcata, FX. (2007). Bovine Whey Proteins - Overview on Their Main Biological Properties. Food Research International, 40, 1197-1211.
  • 19. López-Expósito, I, Manso, MA, López-Fandiño, R, Recio, I. (2008). Activity Against Listeria Monocytogenes of Human Milk During Lactation. A Preliminary Study. Journal of Dairy Research, 7 (1), 24-29.
  • 20. Sarıkaya, SBO, Şişecioğlu, M, Çankaya, M, Gülçin, İ, Ozdemir, H. (2015). Inhibition Profile of A Series of Phenolic Acids on Bovine Lactoperoxidase Enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 30(3), 479-483.
  • 21. Şişecioğlu, M, Uğuz, MT, Çankaya, M, Özdemir, H, Gülçin, İ. (2011). Effects of Ceftazidime Pentahydrate, Prednisolone, Amikacin Sulfate, Ceftriaxone Sodium and Teicoplanin on Bovine Milk Lactoperoxidase Activity. Internatıonal Journal of Pharmacology, 7, 79-83.
  • 22. Shah, A, Lobo, R, Krishnadas, N, Surubhotla, R. (2019). Sesamol and Health-A Comprehensive Review. Indian Journal of Pharmaceutical Education and Research, 53 (2), 28-42.
  • 23. Atmaca,, U, Yıldırım A, Taslimi, P, Tuncel, Çelik S, Gülçin, İ, Supuran,, CT, Çelik, M. (2018). Intermolecular Amination of Allylic and Benzylic Alcohols Leads to Effective Inhibitions of Acetylcholinesterase Enzyme and Carbonic Anhydrase I and II Isoenzymes. Journal of Biochemical and Molecular Toxicology, 32, e22173.
  • 24. Jan, KC, Ho, CT, Hwang, LS. (2008). Bioavailability and Tissue Distribution of Sesamol in Rat. Journal of Agricultural and Food Chemistry, 56, 7032-7037.
  • 25. Bayrak, Ç, Taslimi,, P, Kahraman, HS, Gülçin, İ, Menzek, A. (2019). The First Synthesis, Carbonic Anhydrase Inhibition and Anticholinergic Activities of Some Bromophenol Derivatives with Including Natural Products. Bioorganic Chemistry, 85, 128-139.
  • 26. Topal, M. (2019). The Inhibition Profile of Sesamol Against Α-Glycosidase and Acetylcholinesterase Enzymes. International Journal of Food Properties, 22 (1), 1527-1535.
  • 27. Özyürek, IN, Kalın, R, Özdemir, H. (2020). The Inhibition Effects of D-Penicillamine, D-Penicillamine disulfide and N-Acetyl-D-Penicillamine on Lactoperoxidase Enzyme Activity. Journal of the Institute of Science and Technology, 10 (2), 1146-1153.
Toplam 27 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Konular Sağlık Kurumları Yönetimi
Bölüm Araştırma Makaleleri
Yazarlar

Ramazan Kalın 0000-0002-5917-1299

Yayımlanma Tarihi 2 Ocak 2021
Yayımlandığı Sayı Yıl 2020 Cilt: 9 Sayı: 4

Kaynak Göster

APA Kalın, R. (2021). Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği. Gümüşhane Üniversitesi Sağlık Bilimleri Dergisi, 9(4), 389-395. https://doi.org/10.37989/gumussagbil.790529
AMA Kalın R. Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği. Gümüşhane Sağlık Bilimleri Dergisi. Ocak 2021;9(4):389-395. doi:10.37989/gumussagbil.790529
Chicago Kalın, Ramazan. “Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği”. Gümüşhane Üniversitesi Sağlık Bilimleri Dergisi 9, sy. 4 (Ocak 2021): 389-95. https://doi.org/10.37989/gumussagbil.790529.
EndNote Kalın R (01 Ocak 2021) Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği. Gümüşhane Üniversitesi Sağlık Bilimleri Dergisi 9 4 389–395.
IEEE R. Kalın, “Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği”, Gümüşhane Sağlık Bilimleri Dergisi, c. 9, sy. 4, ss. 389–395, 2021, doi: 10.37989/gumussagbil.790529.
ISNAD Kalın, Ramazan. “Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği”. Gümüşhane Üniversitesi Sağlık Bilimleri Dergisi 9/4 (Ocak 2021), 389-395. https://doi.org/10.37989/gumussagbil.790529.
JAMA Kalın R. Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği. Gümüşhane Sağlık Bilimleri Dergisi. 2021;9:389–395.
MLA Kalın, Ramazan. “Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği”. Gümüşhane Üniversitesi Sağlık Bilimleri Dergisi, c. 9, sy. 4, 2021, ss. 389-95, doi:10.37989/gumussagbil.790529.
Vancouver Kalın R. Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği. Gümüşhane Sağlık Bilimleri Dergisi. 2021;9(4):389-95.