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Laktoperoksidaz Enziminin Keçi Sütünden Saflaştırılması ve Karakterizasyonu, Cefotaxime Sodyumun İnhibisyon Özelliklerinin Araştırılması

Year 2025, Volume: 28 Issue: 2, 298 - 305, 27.03.2025

Metin Tansu Uğuz , Mehmet Muhsin Erol

https://doi.org/10.18016/ksutarimdoga.vi.1532133

Abstract

LPO’ nun doğal bağışıklık için önem arzettiği literatürlerde gösterilmiştir. Bu çalışmanın amacı, keçi sütünden laktoperoksidaz (LPO) enzimini saflaştırmak ve sefotaksim sodyumun enzim üzerindeki inhibisyon özelliğini araştırmaktır. Bu çalışmada, keçi sütünden LPO enzimi saflaştırılmış ve sefotaksim sodyumun inhibisyon etkisi incelenmiştir. Enzim saflaştırma süreçleri çeşitli kromatografik yöntemlerle gerçekleştirilmiş ve enzim inhibitör etkisi Lineweaver-Burk grafikleri ile analiz edilmiştir. Sefotaksim sodyumun enzim üzerindeki inhibisyonu yarışmalı inhibisyon olarak belirlenmiştir. Enzimin keçi sütünden saflaştırılması için, Amberlite CG-50 H+ reçinesiyle kısmi saflaştırma yapılarak, CM-Sephadex C-50 iyon değişim kromatografisi, Sephadex G-100 jel filtrasyon kromatografisi, sırasıyla çalışıldı. ABTS (3-ethylbenzothiazoline-6-sulphonicacid) substratı için Km ve Vmax değerleri ile optimum pH, optimum sıcaklık belirlendi. Enzim saflığı SDS-PAGE elektroforezi ile tespit edildi. Enzimin bir litre keçi sütünden spesifik aktivitesi 7.21 EÜ mg-1 protein miktarı belirlendi. LPO saflaştırma işlemleri sonucunda 1 litre yağı alınmış taze sütten 13.35 kat saflaştırıldı ve 1.9 mg (Rz=0.7) elde edildi. Enzim saflaştırılması sırasında aktivite tayinleri için ABTS substratı (ε412nm=32400M-1 cm-1) kullanıldı.

Keywords

Laktoperoksidaz Kinetik İnhibisyon Sefotaksim Sodyum. Keçi Sütü

Supporting Institution

This study was supported by Bingol University Scientific Research Projects Unit (Project no: BAP-14-95-2011)

Thanks

This study was supported by Bingol University Scientific Research Projects Unit (Project no: BAP-14-95-2011)

References

  • Amornkul, Y., Henning, D.R. (2007). Utilization of microfiltration or Lactoperoxidase system or both for manufacture of Cheddar Cheese from raw milk. Journal Dairy Science, 90, 4988-5000.
  • Barrett, N.E., Grendison, A.S., Lewis, M.J. (1999). Contribution of the lactoperoxidase system to the keeping quality of pasteurized milk. Journal Dairy, 66 (1), 73-75.
  • Boots, J.W., Floris, R. (2006). Lactoperoxidase: From catalytic mechanism to practical applications. A review. İnternational Dairy Journal ,16, 1271-1276.
  • Boroujeni, M.B., Aghamaali, M.R., Nayeri, H., Maal, K.B. (2024). Stabilization of whey lactoperoxidase using betaine. Spectroscopic and computational approaches, 1301, 137329.
  • Brück T.B., Fielding R.J., Symons M.C.R., Harvey P.J. (2001). Eur. J. Biochem, 268, pp. 3214-3222. Daniel, R., Rao, L.D., Mona, IC. (1997). İdentification of colored guaiacol oxidation product produced by peroxidases. Analytical Biochem, 250 (1), 10-17.
  • Doumonted, C., Rousset, B. (1983). İdentification, purification and characterization of a non-heme Lactoperoxidase in bovine milk. Journal Biological Chemistry, 258, 14166-14172.
  • Elegamy, E., Ruppanner, R., İsmail, A., Champagne, C.P., Assal, R. (1992). Purification of lactoperoxidase from bovine whey and investigation of kinetic parameters. Journal Dairy Research, 59, 169-175.
  • Fatemeh, B., Mohammad, M., Jaleh, V., Shariat, S., Seyed, S.S. (2016).  Purification of lactoperoxidase from bovine whey and investigation of kinetic parameters. Advanced Biomedical Research, Mumbai. 5 (1).
  • Gobbetti, M., Minervini, F., Rizzello, C.G. (2004). Angiotensin I-converting-enzyme inhibitory and antimicrobial bioactive peptides. International Journal of Dairy Technology, 57, 173-188.
  • Hashimoto, K., Sato, K., Nakamura, Y., Ohtsuki, K. (2005). Development of a large-scale (50L) apparatus for ampholyte-free isoelectric focusing (autofocusing) of peptides in enzymatic hydrolysates of food proteins. J Agric Food Chem, 53, 3801-3806.
  • Hoogendorn, J.P., Piessens, W., Scholtes, A.S. (1977). Hypothiocyanite ion: The inhibitor formed by the system Lactoperoxidase-thiocyanate-hydrogen peroxide. Caries Research, 11, 77-84.
  • Jacob, B.M., Monoj, N.K., Haridas, M. (1998). Antibacterial property of goat milk Lactoperoxidase. Indian Journal of Experimental Biology, 31, 808.
  • Kandasamy, V.V., Shivanu, S., Rathnasamy, S. (2014). Lactoperoxidase Extraction from Caprine Milk using Conventional and İonic Liquid Based ATP System. İnternational Journal of ChemTech Research, 6 (5), 2887-2893.
  • Koksal, Z., Alim, Z. (2020). Lactoperoxidase, an antimicrobial enzyme, is inhibited by some indazoles. Drug and chemical toxicology, 43 (1), 22–26.
  • Koksal, Z., Kalin, R., Gerni, S., Gulcin, İ., Ozdemir, H. (2017). The inhibition effects of some natural products on lactoperoxidase purified from bovine milk. J. Biochem. Mol. Toxicol, 31(9).
  • Koksal, Z., Usanmaz, H., Bayrak, S., Ozdemir, H. (2017). İmproved chromatographic method for purification of lactoperoxidase from different milk sources. Preparative bıochemistry and biotechnology, 47 (2), 129–136.
  • Kouichirou, S., Hirotoshi, H., Bo, L. (2001). Purification and quantification of lactoperoxidase in human milk with use of immunoadsorbents with antibodies against recombinant human lactoperoxidase. The American Journal of Clinical Nutrition, 73(5), 984-989.
  • Kumar, R., Bhatla, K.L. (1995). Purification, crystallization and preliminary x-ray crystallographic analysis of Lactoperoxidase from buffalo milk. Acta Crystallographica Section D, 51, 1094-1096.
  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951). Protein measurement with the Folin Phenol reagent. Journal of Biological Chemistry, 193, 265-275.
  • Metodiewa, D., Reszka, K., Dunfurd, H.B. (1989). Oxidation of the subsituted catechols dihydroxyphenylalanine methyl ester and trihydroxyphenylalanine by Lactoperoxidase and İts compounds. Archives of Biochemistry and Biophysics, 274, 601.
  • Ozdemir, H., Aygul, I., Kufrevioglu, O.İ. (2001). Purification of Lactoperoxidase from Bovine Milk and Investigation of the Kinetic Properties. Prep. Biochem. Biotechnol, 31, 125–134.
  • Ozdemir, H., Uguz, M. (2005). İn vitro effects of some anaesthetic drugs on Lactoperoxidase enzyme activity. Journal Of Enzyme Inhibition And Medicinal Chemistry, 20, 491-495.
  • Paul, K.G., Ohlsson, P.I. (1985). İn The Lactoperoxidase System: Chemistry and biological significance. Oten. ovue. Journal of Educational Sciences, 15-29.
  • Prince, A., Ratner, A.J (2000). Lactoperoxidase. American Journal of Respiratory Cell and Molecular Biology, 22, 642-644.
  • Pruitt, K.M., Tenovuo, J.O., Andrews, R.W., Mckane, T. (1982). Lactoperoxidase catalysed oxidation of thiocyanate: Polarographic study of the oxidation products. Biochemistry, 21, 562-567.
  • Qin, Y. S., Jiang, H., Wang, C. F., Cheng, M., Wang, L. L., Huang, M. Y., ... & Jiang, H. H. (2021).. J. Dairy Sci., 104 (4), 3936-3946.
  • Reiter, B., Harnulv, G. (1984). Lactoperoxidase antibacterial system: Natural occurence, biological functions and practical applications. Journal of Food Protection, 47, 724-732.
  • Reiter B, Perraudin J-P. (1991). Lactoperoxidase: biological functions. Everse J, Everse KE, Grisham MB (Eds.), Peroxidases in chemistry and biology, 1., CRC Press, Boca Raton, 143-180
  • 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 salivatreated hydroxyapatite in vitro. Caries Res, 28 (6), 421–428.
  • Sarıkaya, B.O., Sisecioglu, M., Cankaya, M., Gulcin, İ.,Ozdemir, H. (2015). Inhibition profile of a series of phenolic acids on bovine lactoperoxidase enzyme. J Enzyme Inhib Med Chem, 30 (3), 479–483.
  • Sarkar S, Misra AK. 1994. Implication of LP-system on manufacture of fermented milk products. Indian Journal Dairy Science, 47 (2), 133-139.
  • Shin, K., Hayasawa, H., Lonnerdal, B. (2001). Inhibition of Escherichia coli respiratory enzymes by the Lactoperoxidase hydrogen peroxide-thiocyanate antimicrobial system. Journal of Applied Microbiology, 90, 489-493.
  • Shindler, J., Bardsley, W.G. (1975). Steady-state kinetics of Lactoperoxidase with ABTS as chromogen. Biochemical and Biophysical Research Communications, 67, 1307-1312.
  • Sisecioglu, M., Cankaya, M., Gulcin, I., Ozdemir, H. (2010). Interactions of melatonin and serotonin to Lactoperoxidase enzyme. Journal Of Enzyme Inhibition And Medicinal Chemistry, 25:, 779-783.
  • Sisecioglu, M., Cankaya, M., Gulcin, I., Ozdemir, H. (2009). The Inhibitory Effect of Propofol on Bovine Lactoperoxidase. Protein and Peptide Letters, 16 (1), 46-49.
  • Sisecioglu M, Gulcin I, Cankaya M, Atasever A, Ozdemir H. (2010b). The effects of norepinephrine on lactoperoxidase enzyme. Scientific Research and Essays, 5, 1351-1356.
  • Sisecioglu, M., Uguz, M.T., Cankaya, M., Ozdemir, H., Gulcin, I. (2011). Effects of ceftazidime pentahydrate, prednisolone, amikacin sulfate, ceftriaxone sodium and teicoplanin on bovine milk lactoperoxidase activity. International Journal of Pharmacology, 7, 79–83.
  • Thomas, E.L., Bozeman, D.B. (1991). Lactoperoxidase: Structure and catalytic properties. In peroxidases in chemistry and biology. Journal Everse K.E., Everse M.B. Grisham Editors. 1, CRC Press. Boca Raton. FL. 123-142.
  • Uguz, M.T., Ozdemir, H. (2005). Purification of bovine milk Lactoperoxidase and investigation of antibacterial properties at different thiocyanate mediated. Applied Biochemistry and Microbiology, 41, 349-353.
  • Wolf S.M, Ferrari RP, Traversa S, Biemann K (2000). Determination of the carbohydrate composition and the disulfide bond linkages of bovine lactoperoxidase by mass spectrometry. J. Mass. Spectrom, 35, 210-217.
  • Wolfson, L.M., Summer, S.A. (1993). Antibacterial activity of the Lactoperoxidase system. A Review Journal of Food Protection, 56, 887-892.
  • Zou, Z., Bauland, J., Hewavitharana, A. K., Al-Shehri, S. S., Duley, J. A., Cowley, D. M., ... & Bansal, N. (2021) A sensitive, high-throughput fluorescent method for the determination of lactoperoxidase activities in milk and comparison in human, bovine, goat and camel milk. Food Chem, 339 Article 128090

Purification and Characterization of Lactoperoxidase from Goat Milk, Investigation of Inhibition Effects of Cefotaxime Sodium

Year 2025, Volume: 28 Issue: 2, 298 - 305, 27.03.2025

Metin Tansu Uğuz , Mehmet Muhsin Erol

https://doi.org/10.18016/ksutarimdoga.vi.1532133

Abstract

İt has been shown in the literature that LPO is important for natural immunity. The purpose of this study is to purify the lactoperoxidase (LPO) enzyme from goat milk and to investigate the inhibition property of cefotaxime sodium on the enzyme. In this study, the LPO enzyme was purified from goat milk and the inhibition effect of cefotaxime sodium was examined. Enzyme purification processes were carried out by various chromatographic methods and the enzyme inhibitory effect was analyzed with Lineweaver-Burk graphs. İnhibition of cefotaxime sodium on LPO was determined as competitive inhibition. The enzyme was purified by first partially purifying milk using Amberlite CG-50 H+ resins, CM-Sephadex C-50 ion-exchange chromatography, and Sephadex G-100 gel filtration chromatography. The 2.2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) substrate was used to determine the enzyme’s Km and Vmax values. Enzyme purity was determined using SDS-PAGE electrophoresis. A specific activity of 7.21 EU mg-1 of protein per liter was detected. The LPO was purified 13.35 times from 1 liter of defatted milk, and 1.9 mg of enzyme was obtained. ABTS substrate (ε412nm=32400M-1 cm-1) was used for the enzyme-activity assays.

Keywords

Goat milk Lactoperoxidase Kinetics Inhibition Cefotaxime Sodium.

References

  • Amornkul, Y., Henning, D.R. (2007). Utilization of microfiltration or Lactoperoxidase system or both for manufacture of Cheddar Cheese from raw milk. Journal Dairy Science, 90, 4988-5000.
  • Barrett, N.E., Grendison, A.S., Lewis, M.J. (1999). Contribution of the lactoperoxidase system to the keeping quality of pasteurized milk. Journal Dairy, 66 (1), 73-75.
  • Boots, J.W., Floris, R. (2006). Lactoperoxidase: From catalytic mechanism to practical applications. A review. İnternational Dairy Journal ,16, 1271-1276.
  • Boroujeni, M.B., Aghamaali, M.R., Nayeri, H., Maal, K.B. (2024). Stabilization of whey lactoperoxidase using betaine. Spectroscopic and computational approaches, 1301, 137329.
  • Brück T.B., Fielding R.J., Symons M.C.R., Harvey P.J. (2001). Eur. J. Biochem, 268, pp. 3214-3222. Daniel, R., Rao, L.D., Mona, IC. (1997). İdentification of colored guaiacol oxidation product produced by peroxidases. Analytical Biochem, 250 (1), 10-17.
  • Doumonted, C., Rousset, B. (1983). İdentification, purification and characterization of a non-heme Lactoperoxidase in bovine milk. Journal Biological Chemistry, 258, 14166-14172.
  • Elegamy, E., Ruppanner, R., İsmail, A., Champagne, C.P., Assal, R. (1992). Purification of lactoperoxidase from bovine whey and investigation of kinetic parameters. Journal Dairy Research, 59, 169-175.
  • Fatemeh, B., Mohammad, M., Jaleh, V., Shariat, S., Seyed, S.S. (2016).  Purification of lactoperoxidase from bovine whey and investigation of kinetic parameters. Advanced Biomedical Research, Mumbai. 5 (1).
  • Gobbetti, M., Minervini, F., Rizzello, C.G. (2004). Angiotensin I-converting-enzyme inhibitory and antimicrobial bioactive peptides. International Journal of Dairy Technology, 57, 173-188.
  • Hashimoto, K., Sato, K., Nakamura, Y., Ohtsuki, K. (2005). Development of a large-scale (50L) apparatus for ampholyte-free isoelectric focusing (autofocusing) of peptides in enzymatic hydrolysates of food proteins. J Agric Food Chem, 53, 3801-3806.
  • Hoogendorn, J.P., Piessens, W., Scholtes, A.S. (1977). Hypothiocyanite ion: The inhibitor formed by the system Lactoperoxidase-thiocyanate-hydrogen peroxide. Caries Research, 11, 77-84.
  • Jacob, B.M., Monoj, N.K., Haridas, M. (1998). Antibacterial property of goat milk Lactoperoxidase. Indian Journal of Experimental Biology, 31, 808.
  • Kandasamy, V.V., Shivanu, S., Rathnasamy, S. (2014). Lactoperoxidase Extraction from Caprine Milk using Conventional and İonic Liquid Based ATP System. İnternational Journal of ChemTech Research, 6 (5), 2887-2893.
  • Koksal, Z., Alim, Z. (2020). Lactoperoxidase, an antimicrobial enzyme, is inhibited by some indazoles. Drug and chemical toxicology, 43 (1), 22–26.
  • Koksal, Z., Kalin, R., Gerni, S., Gulcin, İ., Ozdemir, H. (2017). The inhibition effects of some natural products on lactoperoxidase purified from bovine milk. J. Biochem. Mol. Toxicol, 31(9).
  • Koksal, Z., Usanmaz, H., Bayrak, S., Ozdemir, H. (2017). İmproved chromatographic method for purification of lactoperoxidase from different milk sources. Preparative bıochemistry and biotechnology, 47 (2), 129–136.
  • Kouichirou, S., Hirotoshi, H., Bo, L. (2001). Purification and quantification of lactoperoxidase in human milk with use of immunoadsorbents with antibodies against recombinant human lactoperoxidase. The American Journal of Clinical Nutrition, 73(5), 984-989.
  • Kumar, R., Bhatla, K.L. (1995). Purification, crystallization and preliminary x-ray crystallographic analysis of Lactoperoxidase from buffalo milk. Acta Crystallographica Section D, 51, 1094-1096.
  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951). Protein measurement with the Folin Phenol reagent. Journal of Biological Chemistry, 193, 265-275.
  • Metodiewa, D., Reszka, K., Dunfurd, H.B. (1989). Oxidation of the subsituted catechols dihydroxyphenylalanine methyl ester and trihydroxyphenylalanine by Lactoperoxidase and İts compounds. Archives of Biochemistry and Biophysics, 274, 601.
  • Ozdemir, H., Aygul, I., Kufrevioglu, O.İ. (2001). Purification of Lactoperoxidase from Bovine Milk and Investigation of the Kinetic Properties. Prep. Biochem. Biotechnol, 31, 125–134.
  • Ozdemir, H., Uguz, M. (2005). İn vitro effects of some anaesthetic drugs on Lactoperoxidase enzyme activity. Journal Of Enzyme Inhibition And Medicinal Chemistry, 20, 491-495.
  • Paul, K.G., Ohlsson, P.I. (1985). İn The Lactoperoxidase System: Chemistry and biological significance. Oten. ovue. Journal of Educational Sciences, 15-29.
  • Prince, A., Ratner, A.J (2000). Lactoperoxidase. American Journal of Respiratory Cell and Molecular Biology, 22, 642-644.
  • Pruitt, K.M., Tenovuo, J.O., Andrews, R.W., Mckane, T. (1982). Lactoperoxidase catalysed oxidation of thiocyanate: Polarographic study of the oxidation products. Biochemistry, 21, 562-567.
  • Qin, Y. S., Jiang, H., Wang, C. F., Cheng, M., Wang, L. L., Huang, M. Y., ... & Jiang, H. H. (2021).. J. Dairy Sci., 104 (4), 3936-3946.
  • Reiter, B., Harnulv, G. (1984). Lactoperoxidase antibacterial system: Natural occurence, biological functions and practical applications. Journal of Food Protection, 47, 724-732.
  • Reiter B, Perraudin J-P. (1991). Lactoperoxidase: biological functions. Everse J, Everse KE, Grisham MB (Eds.), Peroxidases in chemistry and biology, 1., CRC Press, Boca Raton, 143-180
  • 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 salivatreated hydroxyapatite in vitro. Caries Res, 28 (6), 421–428.
  • Sarıkaya, B.O., Sisecioglu, M., Cankaya, M., Gulcin, İ.,Ozdemir, H. (2015). Inhibition profile of a series of phenolic acids on bovine lactoperoxidase enzyme. J Enzyme Inhib Med Chem, 30 (3), 479–483.
  • Sarkar S, Misra AK. 1994. Implication of LP-system on manufacture of fermented milk products. Indian Journal Dairy Science, 47 (2), 133-139.
  • Shin, K., Hayasawa, H., Lonnerdal, B. (2001). Inhibition of Escherichia coli respiratory enzymes by the Lactoperoxidase hydrogen peroxide-thiocyanate antimicrobial system. Journal of Applied Microbiology, 90, 489-493.
  • Shindler, J., Bardsley, W.G. (1975). Steady-state kinetics of Lactoperoxidase with ABTS as chromogen. Biochemical and Biophysical Research Communications, 67, 1307-1312.
  • Sisecioglu, M., Cankaya, M., Gulcin, I., Ozdemir, H. (2010). Interactions of melatonin and serotonin to Lactoperoxidase enzyme. Journal Of Enzyme Inhibition And Medicinal Chemistry, 25:, 779-783.
  • Sisecioglu, M., Cankaya, M., Gulcin, I., Ozdemir, H. (2009). The Inhibitory Effect of Propofol on Bovine Lactoperoxidase. Protein and Peptide Letters, 16 (1), 46-49.
  • Sisecioglu M, Gulcin I, Cankaya M, Atasever A, Ozdemir H. (2010b). The effects of norepinephrine on lactoperoxidase enzyme. Scientific Research and Essays, 5, 1351-1356.
  • Sisecioglu, M., Uguz, M.T., Cankaya, M., Ozdemir, H., Gulcin, I. (2011). Effects of ceftazidime pentahydrate, prednisolone, amikacin sulfate, ceftriaxone sodium and teicoplanin on bovine milk lactoperoxidase activity. International Journal of Pharmacology, 7, 79–83.
  • Thomas, E.L., Bozeman, D.B. (1991). Lactoperoxidase: Structure and catalytic properties. In peroxidases in chemistry and biology. Journal Everse K.E., Everse M.B. Grisham Editors. 1, CRC Press. Boca Raton. FL. 123-142.
  • Uguz, M.T., Ozdemir, H. (2005). Purification of bovine milk Lactoperoxidase and investigation of antibacterial properties at different thiocyanate mediated. Applied Biochemistry and Microbiology, 41, 349-353.
  • Wolf S.M, Ferrari RP, Traversa S, Biemann K (2000). Determination of the carbohydrate composition and the disulfide bond linkages of bovine lactoperoxidase by mass spectrometry. J. Mass. Spectrom, 35, 210-217.
  • Wolfson, L.M., Summer, S.A. (1993). Antibacterial activity of the Lactoperoxidase system. A Review Journal of Food Protection, 56, 887-892.
  • Zou, Z., Bauland, J., Hewavitharana, A. K., Al-Shehri, S. S., Duley, J. A., Cowley, D. M., ... & Bansal, N. (2021) A sensitive, high-throughput fluorescent method for the determination of lactoperoxidase activities in milk and comparison in human, bovine, goat and camel milk. Food Chem, 339 Article 128090
There are 42 citations in total.

Details

Primary Language English
Subjects Biochemistry and Cell Biology (Other)
Journal Section RESEARCH ARTICLE
Authors

Metin Tansu Uğuz 0000-0002-3557-1677

Mehmet Muhsin Erol 0009-0009-3660-0271

Early Pub Date March 20, 2025
Publication Date March 27, 2025
Submission Date August 13, 2024
Acceptance Date January 17, 2025
Published in Issue Year 2025 Volume: 28 Issue: 2

Cite

APA Uğuz, M. T., & Erol, M. M. (2025). Purification and Characterization of Lactoperoxidase from Goat Milk, Investigation of Inhibition Effects of Cefotaxime Sodium. Kahramanmaraş Sütçü İmam Üniversitesi Tarım Ve Doğa Dergisi, 28(2), 298-305. https://doi.org/10.18016/ksutarimdoga.vi.1532133
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