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Sülfamat iskeleti içeren birçok doğal ürün ve ilaç etken maddelerinde bulunmaktadırlar. Son zamanlarda, sülfamatlar bileşiklerinin bulundurdukları fonksiyonel gruplarından dolayı malzeme bilimcisi ve farmakolog tarafından daha fazla ilgi görmektedirler. Peroksidazlar (POD), metabolik fonksiyonlarından dolayı gıda ve ilaç endüstrisinde enzimatik reaksiyonlarda ve klinik teşhislerde önemli kullanım alanında yer alırlar. Laktoperoksidaz (LPO, EC 1.11.1.7 ) peroksidaz ailesinin bir üyesidir. Bu enzim sütte, tükürükte ve gözyaşında bulunan bir oksidoredüktaz olup, patojen mikroorganizmalara karşı yeni doğanların bağırsak sistemlerini ve meme bezlerini korumada önemli bir role sahiptir. Memeli sütlerinden edilen LPO enzimi, bakterilerin büyümesinin baskılanmasında ve bakteri inhibisyonunun desteklenmesinde oldukça önemlidir. Sığır LPO’sunun bakteriyal büyümeyi inhibe etmesi, H2O2 ve tiyosiyanat içeren peroksidaz sistemine atfedilir. Bu sistemin antimikrobiyal etkisi sütte doğal olarak oluşur. LPO enzimi üzerine yapılan antibakteriyal çalışmalarda LPO-tiyosiyanat ve peroksit sisteminin patajonik bakterilerde önemli derecede inhibisyona sebep olduğu tespit edilmiştir. LPO’nun birçok uygulama alanı vardır. Peroksidazlar hem gıdalarda hem de farmakolojik uygulamalarda koruyucu olarak kullanılabilmekte ve süt işleme tesislerinde nakil esnasında sütün muhafazası amacıyla süt endüstrisinde kullanılmaktadır. Bu çalışmanın amacı, LPO enzimi üzerine Metil benzoilsülfamat, Metil (2-bromobenzoil)sülfamat, Metil (3-fenilpropanoil)sülfamat, Metil (1-naphthoil)sülfamat, Metil (2-metilbenzoil)sülfamat, Metil (2-iyodobenzoil)sülfamat, Metil (2-fenilbutanoil)sülfamat, Metil (4-isopropilbenzoil)sülfamat, Metil (4-metoksibenzoil)sülfamat ve Metil (isoquinoline-1-karbonil)sülfamat bileşilklerinin in vitro etkilerini belirlemektir. Bu sülfamat türevi bileşiklerinin LPO enzimi üzerindeki inhibisyon etkisini belirlemek için, enzim aktiviteleri ölçülerek her bir inhibitör için Lineweaver-Burk grafikleri çizildi; Ki sabiti ve inhibisyon tipleri bu çizilen grafiklerden hesaplandı. Ki değerleri sırasıyla Metil benzoilsülfamat 0,70 μM, Metil (2-bromobenzoil)sülfamat 0,025 μM, Metil (3-fenilpropanoil)sülfamat 0,018 μM, Metil (1-naphthoil)sülfamat 0,047 μM, Metil (2-metilbenzoil)sülfamat 0,043 μM, Metil (2-iyodobenzoil)sülfamat 0,19 μM, Metil (2-fenilbutanoil)sülfamat 0,39 μM, Metil (4-isopropilbenzoil)sülfamat 0,42 μM, Metil (4-metoksibenzoil)sülfamat 0,078 μM, Metil (isoquinoline-1-karbonil)sülfamat 0,075 μM olarak belirlendi. Metil (4-isopropilbenzoil)sülfamat bileşiği yarışmasız inhibisyon ve diğer maddeler yarışmalı inhibisyon gösterdiği kaydedildi. Metil (2-metilbenzoil)sülfamat bileşiği ise en etkili inhibitör özelliğini yarışmalı inhibisyon tipi LPO enzimi üzerine 0.018 ± 0.024 μM Ki değeri ile göstermiştir.
They are found in many natural products and medicinal ingredients that contain sulfate skeleton. Recently, sulfates have gained greater interest by material scientists and pharmacologists due to their functional groups in which they contain compounds. Peroxidazes (PODs) are important in enzymatic reactions and clinical diagnosis in the food and pharmaceutical industry due to their metabolic functions. Lactoperoxidase (LPO, EC 1.11.1.7) is a member of the peroxidase family. This enzyme is an oxideductaze found in milk, sperm and tears, and has an important role in protecting the intestinal systems and breast glands of newborns against pathogenic microorganisms. The LPO enzyme derived from breast milk is very important in suppressing bacterial growth and supporting bacterial inhibition. The beef LPO inhibits bacterial growth, is attributed to the peroxydase system containing H2O2 and tiyosyanate. The antimicrobial effect of this system occurs naturally in milk. Antibacterial studies on the LPO enzyme have found that the LPO-tiyosyanate and peroxide systems cause substantial inhibition in pathogenous bacteria. LPO has many areas of application. Peroxidazes can be used as protective in both food and pharmacological applications and are used in the dairy industry for the purpose of milk conservation during transplantation in dairy processing facilities. The aim of this study on the LPO enzyme is to determine the in vitro effects of methyl benzoyl sulfate, methyl (2-bromobenzoil)sulfate, methyl (3-fenylpropanoil)sulfate, methyl (1-naphthoil)sulfate, methyl (2-methylbenzoil)sulfate, methyl (2-iyodobenzoil)sulfate, methyl (2-fenylbutanoil)sulfate, methyl (4-isopropylbenzoil)sulfate, methyl (4-methoksibenzoil)sulfate and methyl (isocinoline-1-carbonil)sulfate compounds. To determine the inhibition effect of these sulfate derivative compounds on the LPO enzyme, Lineweaver-Burk graphs for each inhibitor were drawn by measuring the enzyme activity; which stability and inhibition types were calculated from these drawn graphs. What values are methyl benzoyl sulfate 0.70 μM, methyl (2-bromobenzoil)sulfate 0.025 μM, methyl (3-fenylpropanoil)sulfate 0.018 μM, methyl (1-naphthoil)sulfate 0.047 μM, methyl (2-methylbenzoil)sulfate 0.043 μM, methyl (2-iyodobenzoil)sulfate 0.19 μM, methyl (2-fenylbutanoil)sulfate 0.39 μM, methyl (4-isopropilbenzoil)sulfate 0.42 μM, methyl (4-methylbenzoil)sulfate 0.078 μM, methyl (methylbenzoil-1)sulfate 0.75 μM. Methyl (4-isopropylbenzoil)sulfate compound has been
They are found in many natural products and active ingredients that contain a sulfamate skeleton. Recently, due to the functional groups of sulfamates compounds, they have received more attention from the material scientist and pharmacologist. Due to their metabolic functions, peroxidases (POD) are important in enzymatic reactions and clinical diagnoses in the food and pharmaceutical industry. Lactoperoxidase (LPO, EC 1.11.1.7) is a member of the peroxidase family. This enzyme is an oxidoreductase found in milk, saliva and tears and has an important role in protecting the gut systems and mammary glands of newborns against pathogenic microorganisms. The LPO enzyme from mammalian milk is very important in suppressing the growth of bacteria and promoting bacterial inhibition. Inhibition of bacterial growth of bovine LPO is attributed to the peroxidase system containing H2O2 and thiocyanate. The antimicrobial effect of this system occurs naturally in milk. In antibacterial studies on LPO enzyme, LPO-thiocyanate and peroxide system has been found to cause a significant inhibition of pathogenic bacteria. LPO has many application areas. Peroxidases can be used as preservatives in both food and pharmacological applications, and are used in the milk industry for milk preservation during transport in milk processing plants. The aim of this study is to determine the in vitro effects of Methyl benzoylsulfamate, Methyl (2-bromobenzoyl) sulfamate, Methyl (3-phenylpropanoyl) sulfamate, Methyl (1-naphthoyl) sulfamate, Methyl (2-methylbenzoyl) sulfamate, Methyl (2-iodobenzoyl) sulfamate, Methyl (2-phenyl), Methyl (4-isopropylbenzoyl) sulfamate, Methyl (4-methoxybenzoyl) sulfamate and Methyl (isoquinoline-1-carbonyl) sulfamate compounds on LPO enzyme. To determine the inhibition effect of these sulfamate derivative compounds on the LPO enzyme, Lineweaver-Burk plots were drawn for each inhibitor by measuring enzyme activities; Ki constant and inhibition types were calculated from these plotted graphs. Ki values were determined as Methyl benzoylsulfamate 0.70 μM, Methyl (2-bromobenzoyl) sulfamate 0.025 μM, Methyl (3-phenylpropanoyl) sulfamate 0.018 μM, Methyl (1-naphthoyl) sulfamate 0.047 μM, Methyl (2-methylbenzoyl) sulfamate 0.043 μM, Methyl (2-methylbenzoyl) sulfamate 0.043 μM -Iodobenzoyl) sulfamate 0.19 μM, Methyl (2-phenylbutanoyl) sulfamate 0.49 μM, Methyl (4-isopropylbenzoyl) sulfamate 0.42 μM, Methyl (4-methoxybenzoyl) sulfamate 0.078 μM, Methyl (isoquinoline-1-carbonyl ) sulfamate 0.075 μM, respectively. Methyl (4-isopropylbenzoyl) sulfamate compound was noted to exhibit non-competitive inhibition and other substances showed competitive inhibition. Methyl (2-methylbenzoyl) sulfamate compound, on the other hand, showed its most effective inhibitory feature on competitive competitive inhibition type LPO enzyme with a value of Ki 0.018 ± 0.024 μM.
Alan : Fen Bilimleri ve Matematik; Mühendislik
Dergi Türü : Uluslararası
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