Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes

Yıl: 2018 Cilt: 39 Sayı: 33 Sayfa Aralığı: 828 - 832 Metin Dili: İngilizce DOI: 10.17776/csj.452514 İndeks Tarihi: 22-01-2020

Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes

Öz:
The vast majority of the carbohydrates in the biomolecule class are formed by photosynthesis using sunlight. One of the important enzymes in this class is α-glycosidase. This enzyme converts complex carbohydrates to monosaccharides. On the other hand, another important enzyme species is the α-amylase enzyme. Which directly related to starch. Starch is a type of polymer formed by the oxygen binding of glucose units to each other at the C1 position with glycosidic bonds. α-Amylase is an enzyme that catalyzes the hydrolysis of glycosidic bonds in starch, and this enzyme is purified from a wide variety of animals, plants, and microorganisms. Resorcinol, a phenol derivative, is an important organic chemical substance in the production of textile, medicine, hair dye, plastic and agricultural products of many industrial materials. Resorcinol, a phenol derivative, is present as white crystals, and resorcinol consists of two hydroxyl molecules attached to the benzene ring, and also was defined as α-glycosidase and α-amylase inhibitor to detect antidiabetic properties. Resorcinol was used as 𝛼-glycosidase and 𝛼-amylase inhibitor. Accordingly, IC50 values of α-amylase and α-glycosidase were calculated as 1.34 μM and 77.00 nM, respectively. On the other hand, Ki value for α-glycosidase was found as 30.16 nM. It has been observed that α-amylase and α-glycosidase enzymes can inhibit by resorcinol compound. It has the properties of inhibiting carbohydrate absorption by inhibiting α-glycosidase enzymes in the small intestine. For both metabolic enzymes, resorcinol may be preferred as an inhibitor. In this case, resorcinol may be used as an inhibitor against to healty problems like Diabetes mellitus and antiobesity.
Anahtar Kelime:

Antidiyabetik Potansiyel: Resorsinol’ün α-Glukozidaz ve α-Amilaz Enzimleri Üzerine Etkisi

Öz:
Biyomolekül sınıfında bulunan karbohidratların büyük çoğunluğu güneş ışığını kullanarak fotosentez sonucu oluşurlar. Bu sınıfın önemli enzimlerinden birisi ise 𝛼-Glikozidaz dır. Bu enzim, kompleks karbohidratları monosakkaritlere dönüştürür. Diğer taraftan bir başka önemli enzim türü ise α-amilaz enzimidir. Bu enzim ise nişasta ile doğrudan ilişkilidir. Nişasta, glukoz ünitelerinin birbirine glikozidik bağlarla C1 pozisyonunda yer alan oksijenden bağlanmasıyla oluşan bir polimer türüdür. α-Amilaz, nişastada bulunan bu glikozidik bağların hidrolizini katalizleyen enzimlerdir ve bu enzim çok çeşitli hayvan, bitki ve mikroorganizmalardan saflaştırılmaktadır. Bir fenol türevi olan resorsinol, birçok endüstriyel malzemelerin tekstil, ilaç, saç boyaları, plastik ve tarım ürünlerinin üretiminde önemli bir organik kimyasal maddedir. Fenol türevi olan resorsinol beyaz kristaller halinde bulunur ve resorsinol benzen halkasına bağlı iki hidroksil molekülünden oluşur. 𝛼-Glikozidaz ve 𝛼-amilaz inhibitörü olarak resorsinol kullanıldı. Buna göre α-amilaz ve α-glikosidaz, sırasıyla IC50 değerleri 1,34 μM ve 77,00 nM olarak hesaplandı. Öte yandan, α-glikosidaz için Ki değeri 30,16 nM olarak bulundu. 𝛼-Amilaz ve 𝛼-glikozidaz enzimlerini resorsinol bileşiği inhibe edebildiği gözlemlendi. İnce barsakta 𝛼-glukozidaz enzimlerini inhibe ederek karbohidrat emilimini geciktirme özelliklerine sahiptirler. Her iki metabolik enzim için resorsinol, bir inhibitör olarak tercih edilebilir. Bu durumda resorsinol, Diyabet mellitus ve antiobezite gibi sağlık sorunlarına karşı inhibitör olarak kullanılabilir.
Anahtar Kelime:

Belge Türü: Makale Makale Türü: Araştırma Makalesi Erişim Türü: Erişime Açık
  • Taslimi P. and Gulcin I., Antidiabetic potential: in vitro inhibition effects of some natural phenolic compounds on α- glycosidase and α-amylase enzymes, Journal of Biochemical and Molecular Toxicology, 31(2017), e21956.
  • Cengiz Ecemis G. and Atmaca H., Oral antidiabetic agents, Journal of Experimental and Clinical Medicine, 29(2012), 23-29.
  • Tuzlakoglu Ozturk M., Yerel bacillus İzolatlarından alfa Amilazların Klonlanması ve Rekombinant amy28 alfa Amilazının Enzim Özelliklerinin Belirlenmesi, Gebze Yüksek Teknoloji Enstitüsü Mühendislik ve Fen Bilimleri Enstitüsü, Doktora Tezi, Gebze (2013).
  • Oztolan O., Alfa Amilaz-Dekstran Konjugatlarının Sentezi Ve Karakterizasyonu, Yıldız Teknik Üniversitesi Fen Bilimleri Enstitüsü, Yüksek Lisans Tezi, İstanbul (2007).
  • Xiao, Z., Storms, R. and Tsang, A., A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities. Analytical Biochemistry, 351(2006), 146-148.
  • Taslimi P., Akıncıoğlu H. and Gulcin I., Synephrine and phenylephrine act as α- amylase, α-glycosidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase enzymes inhibitors. Journal of Biochemical and Molecular Toxicology, 31(2017), 11, e21973.
  • Uysal A., Zengin G., Durak Y. and Aktumsek A., Centaurea pterocaula özütlerinin antioksidan ve antimutajenik özellikleri ile enzim inhibitör potansiyellerinin incelenmesi. Marmara Pharmaceutical Journal, 20(2016), 232- 242.
  • Enache TA. and Oliveira-Brett AM., Phenol and parasubstituted phenols electrochemical oxidation pathways, Journal of Electroanalytical Chemistry, 655(2011), 9-16.
  • Salazar R., Vidal J., Martínez-Cifuentes M., Araya-Maturana R. and Ramírez- Rodríguez O., Electrochemical characterization of hydroquinone derivatives with different substituents in acetonitrile, New Journal of Chemistry, 39(2015), 1237-1246.
  • Dunlap T,, Chandrasena REP., Wang Z., Sinha V., Wang Z. and Thatcher GRJ., Quinone Formation as a Chemoprevention Strategy for Hybrid Drugs: Balancing Cytotoxicity and Cytoprotection, Chemical Research Toxicology, 20(2007), 1903-1912.
  • Zhang Z., Yuan Lian X., Li S.and Stringer JL., Characterization of chemical ingredients and anticonvulsant activity of American skullcap (Scutellaria lateriflora), Phytomedicine, 16(2009), 485-493.
  • Tao Y., Zhang Y., Cheng Y. and Wang Y., Rapid screening and identification of α-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR, Biomedical Chromatography, 27(2013), 148-155.
  • Xiao Z., Storms R. and Tsang A., A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities, Analytical Biochemistry, 351(2006), 146-8.
  • Varan G., Yeni Tanı Almış Prediyabetik ve Diyabetik Hastalarda Akarboz Kullanımının Metabolik Parametreler Üzerine Etkisi, Mustafa Kemal Üniversitesi Tayfur Ata Sökmen Tıp Fakültesi, Uzmanlık Tezi, Hatay (2015).
  • Teng H., Chen L., Fang T., Yuan B. and Lin Q., Rb2 inhibits a-glucosidase and regulates glucose metabolism by activating AMPK pathways in HepG2 cells, Journal of Functional Foods, 28(2017), 306-313.
  • Torres-Naranjo M., Suárez A., Gilardoni G., Cartuche L., Flores P. and Morocho V., Chemical Constituents of Muehlenbeckia tamnifolia (Kunth) Meisn (Polygonaceae) and Its In Vitro α-Amilase and α-Glucosidase Inhibitory Activities, Molecules, 21(2016), 1461.
APA Topal F (2018). Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. , 828 - 832. 10.17776/csj.452514
Chicago Topal Fevzi Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. (2018): 828 - 832. 10.17776/csj.452514
MLA Topal Fevzi Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. , 2018, ss.828 - 832. 10.17776/csj.452514
AMA Topal F Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. . 2018; 828 - 832. 10.17776/csj.452514
Vancouver Topal F Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. . 2018; 828 - 832. 10.17776/csj.452514
IEEE Topal F "Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes." , ss.828 - 832, 2018. 10.17776/csj.452514
ISNAD Topal, Fevzi. "Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes". (2018), 828-832. https://doi.org/10.17776/csj.452514
APA Topal F (2018). Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. Cumhuriyet Science Journal, 39(33), 828 - 832. 10.17776/csj.452514
Chicago Topal Fevzi Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. Cumhuriyet Science Journal 39, no.33 (2018): 828 - 832. 10.17776/csj.452514
MLA Topal Fevzi Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. Cumhuriyet Science Journal, vol.39, no.33, 2018, ss.828 - 832. 10.17776/csj.452514
AMA Topal F Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. Cumhuriyet Science Journal. 2018; 39(33): 828 - 832. 10.17776/csj.452514
Vancouver Topal F Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes. Cumhuriyet Science Journal. 2018; 39(33): 828 - 832. 10.17776/csj.452514
IEEE Topal F "Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes." Cumhuriyet Science Journal, 39, ss.828 - 832, 2018. 10.17776/csj.452514
ISNAD Topal, Fevzi. "Antidiabetic Potential: Effect of Resorcinol on α-Glycosidase and α-Amylase Enzymes". Cumhuriyet Science Journal 39/33 (2018), 828-832. https://doi.org/10.17776/csj.452514