Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions

Karaderi, Cennet Canan; KAHRAMAN, Hüseyin

doi:10.46810/tdfd.1233931

Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions

Cennet Canan KARADERİ, (İnönü Üniversitesi, Fen Bilimleri Enstitüsü, Biyoloji Bölümü, Malatya, Türkiye)

Hüseyin KAHRAMAN (İnönü Üniversitesi, Fen Edebiyat Fakültesi , Biyoloji Bölümü, Malatya, Türkiye)

Türk Doğa ve Fen Dergisi

3 1

Yıl: 2023 Cilt: 12 Sayı: 2 Sayfa Aralığı: 99 - 103 Metin Dili: İngilizce DOI: 10.46810/tdfd.1233931 İndeks Tarihi: 08-08-2023

Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions

Öz:

Prokaryotes form an important part of our lives. These microorganisms, which we can not see with the naked eye, are used in medicine, biotechnology, microbiology and many other fields. They can produce many anti-cancer enzymes (Arginine deiminase, Asparaginase, Methionine gamma lyase etc.). In this study, an important bacterial anti-tumor enzyme of B. cereus and R. eutropha in the presence of different minimal sources (Dextrose, Fructose, Glucose, Xylose, Maltose, Nutrient Broth, Rhamnose, Ribose, Sucrose) under static and shaking (150 rpm) conditions. Arginine deiminase activity was searched. In accordance with results of our study, these microorganisms showed the highest ADI activity in the disaccharide medium, maltose and sucrose, and in the aldose group, in the ribose medium. It has been shown that this enzyme, which is used in cancer treatment, can be produced more cheaply and easily in minimal environments.

Anahtar Kelime: Bacillus cereus Ralstonia eutropha Arginine deiminase

Minimal Koşullar Altında Bacillus cereus ve Ralstonia eutropha' da Arjinin deiminaz (ADI) Aktivitesinin Araştırılması

Öz:

Prokaryotlar, hayatımızın önemli bir parçasını oluşturmaktadır. Çıplak göz ile göremediğimiz bu mikroorganizmalar tıp, biyoteknoloji, mikrobiyoloji ve daha pek çok alanda kullanılmaktadır. Pek çok anti kanser enzimlerini (Arjinin deiminaz, Asparaginaz, Metiyonin gama liyaz vb) üretebilmektedirler. Bu çalışmada B. cereus ve R. eutropha’ nın statik ve çalkalamalı (150 rpm) koşullarda, farklı minimal kaynakları (Dekstroz, Fruktoz, Glukoz, Ksiloz, Maltoz, Nutrient Broth Ramnoz, Riboz, Sükroz) varlığında önemli bir bakteriyel anti-tümör enzimi olan ADI aktivitesi araştırılmıştır. Çalışmanın sonuçlarına göre bu mikroorganizmalar, disakkarit ortamlarında maltoz ve sükroz, aldoz grubunda ise riboz ortamında en yüksek ADI aktivitesi göstermiştir. Kanser tedavisinde kullanılan bu enzimin minimal ortamlarda, daha ucuz, kolay bir şekilde üretilebileceği gösterilmiştir.

Anahtar Kelime: Bacillus cereus Ralstonia eutropha Arjinin deiminaz

Belge Türü: Makale Makale Türü: Araştırma Makalesi Erişim Türü: Erişime Açık

[1] Iqbal J., Abbasi B.A., Mahmood T., Kanwal S., Ali B., Shah S.A., Khalil A.T. Plant-derived anticancer agents: A green anticancer approach, Asian Pac J Trop Biomed. 2017; 7(12): 1129–1150.
[2] Al Koussa H., El Mais N., Maalouf H., Abi Habib R., El Sibai M. Arginine deprivation: a potential therapeutic for cancer cell metastasis? A review, Cancer Cell Inter. 2020; 20(150): 1-7.
[3] Prajapati B., Supriya N. R. Review on anticancer enzymes and their targeted amino acids, World J Pharm Res, 2017; 6(12), 268-284.
[4] Zolfaghar M., Amoozegar M. A., Khajeh K., Babavalian H., Tebyanian H. Isolation and screening of extracellular anticancer enzymes from halophilic and halotolerant bacteria from different saline environments in Iran, Mol Biol Rep, 2019; 46: 3275–3286.
[5] Özalp Erenler Ş. L-asparaginaz geninin (ansB) farklı gram-negatif bakterilere klonlanması, izolasyonu ve ekspresyonu (Doktora tezi). 2007; İnönü Üniversitesi, Fen Bilimleri Enstitüsü, Malatya
[6] Zarei M., Nezafat N., Rahbar M.R., Negahdaripour M., Sabetian S., Morowvat M.H., Ghasemi Y. Decreasing the immunogenicity of arginine deiminase enzyme via structure based computational anal ysis, J Biomol Structure and Dynamics. 2019; 37(2): 523-536.
[7] Kahraman H., Karaderi C.C., The Importance of Arginine deiminase, Arch Chem and Chem Eng. 2019; 1(1): 1-3.
[8] Cheng F., Yang J., Schwaneberg U., Zhu L. Rational surface engineering of an arginine deiminase (an antitumor enzyme) for increased PEGylation efficiency, Biotechnol Bioeng. 2019;116: 2156–2166.
[9] Szefel J., Danielak A., Kruszewski W.J. Metabolic pathways of L-arginine and therapeutic consequences in tumors, Adv in Med Sci. 2019; 64:104-110.
[10] Zou S., Wang X., Liu P., Ke C., Xu S. Arginine metabolism and deprivation in cancer therapy, Biomed Pharm. 2019; 118:1-11.
[11] Zaki Mahdi N. Investigation of the lethal effect of purified Arginine deiminase purified from Lactobacillus plantarum p5 on murine mammary adenocarcinoma and vero cell lines, Archives of Razi Institu, 2022; 77(1): 223-229.
[12] Kaur B., Kaur R. Application of Response Surface Methodology for Optimizing Arginine deiminase Production Medium for Enterococcus faecium sp. GR7, The Sci World J. 2013; 1-12.
[13] Mahdy N.Z., Al-Tahan S.S., Yaseen N.Y., Optimization of Arginine deiminase production from a local higher productive isolate Enterococcus faecium M1, Iraqi J Cancer and Med Genet, 2014; 7(1):36-43.
[14] Karaderi C.C., Kahraman H. Trehalose Production at Different Mediums in Bacillus cereus and Ralstonia eutropha, Acta Sci Agricul. 2021; 5(10): 2-4.
[15] Juengert J.R., Borisova M., Mayer C., Wolz C., Brigham C.J., Sinskey A.J., Jendrossek D. Absence of ppGpp leads to increased mobilization of intermediately accumulated Poly (3- Hydroxybutyrate) in Ralstonia eutropha H16, Appl Environ Microbiol. 2017; 83(13): 1-17.
[16] Arenas López, C., Locker, J., Orol, D., Walter, F., Busche, T., Kalinowski, J., Minton, N.P., Kovács, K., Winzer, K., The genetic basis of 3 hydroxypropanoate metabolism in Cupriavidus necator H16, Biotechnol for Biofuels. 2019; 12(150): 1-16.
[17] Karaderi, C.C., Bakterilerin Farklı Karbon Kaynaklarının Varlığında Arjinin deiminaz, Trehalaz ve Poli Hidroksi Bütirat Üretiminin Araştırılması (Doktora Tezi), İnönü Üniversitesi, Malatya. 2022.
[18] Takahara H., Okamoto H., Sugawara K. Enzymatic assay of peptidyl Arginine deiminase, J Biochem. 1986; 99:1417- 1424.
[19] Sharma A., Bala K., Husain I. Optimization of Arginine Deaminase production from Indigenous bacterium Pseudomonas aeruginosa PS2, Int J Curr Microbiol Appl Sci. 2017; 6(11): 3621-3632.
[20] Dhankhar R., Kumar A., Kumar S., Chhabra D., Shukla P., Gulati P. Multilevel algorithms and evolutionary hybrid tools for enhanced production of arginine deiminase from Pseudomonas furukawaii RS3, Bioresour Technol. 2019; 290: 1- 9.
[21] Mahdy N.Z., Al-Tahan S.S., Yaseen N.Y. Optimization of arginine deiminase production from a local higher productive isolate Enterococcus faecium M1, Iraqi J Cancer Med Genet, 2014; 7(1): 36-43.
[22] Ibrahim R.A., Hussein A.A., Abdulwahed S. Optimizing arginine deiminase production from Pseudomonas aeruginosa clinical isolate, J Pharm Sci Res, 2019; 11(2): 656-660.
[23] Khaleed Shaikh A.N., Khobragade R.M. Production and partial purification of arginine deiminase isolated from bacteria, J Emerg Technol Innov Res, 2019; 6(3): 241-248.
[24] Unissa R., Sudhakar M., Kumar Reddy A.S. Condition optimization and production of extracellular l-Arginine deiminase from Vibrio alginolyticus 1374, Curr Biotechnol, 2015; 4: 254- 260

APA	Karaderi C, KAHRAMAN H (2023). Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. , 99 - 103. 10.46810/tdfd.1233931
Chicago	Karaderi Cennet Canan,KAHRAMAN Hüseyin Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. (2023): 99 - 103. 10.46810/tdfd.1233931
MLA	Karaderi Cennet Canan,KAHRAMAN Hüseyin Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. , 2023, ss.99 - 103. 10.46810/tdfd.1233931
AMA	Karaderi C,KAHRAMAN H Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. . 2023; 99 - 103. 10.46810/tdfd.1233931
Vancouver	Karaderi C,KAHRAMAN H Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. . 2023; 99 - 103. 10.46810/tdfd.1233931
IEEE	Karaderi C,KAHRAMAN H "Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions." , ss.99 - 103, 2023. 10.46810/tdfd.1233931
ISNAD	Karaderi, Cennet Canan - KAHRAMAN, Hüseyin. "Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions". (2023), 99-103. https://doi.org/10.46810/tdfd.1233931

APA	Karaderi C, KAHRAMAN H (2023). Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. Türk Doğa ve Fen Dergisi, 12(2), 99 - 103. 10.46810/tdfd.1233931
Chicago	Karaderi Cennet Canan,KAHRAMAN Hüseyin Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. Türk Doğa ve Fen Dergisi 12, no.2 (2023): 99 - 103. 10.46810/tdfd.1233931
MLA	Karaderi Cennet Canan,KAHRAMAN Hüseyin Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. Türk Doğa ve Fen Dergisi, vol.12, no.2, 2023, ss.99 - 103. 10.46810/tdfd.1233931
AMA	Karaderi C,KAHRAMAN H Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. Türk Doğa ve Fen Dergisi. 2023; 12(2): 99 - 103. 10.46810/tdfd.1233931
Vancouver	Karaderi C,KAHRAMAN H Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions. Türk Doğa ve Fen Dergisi. 2023; 12(2): 99 - 103. 10.46810/tdfd.1233931
IEEE	Karaderi C,KAHRAMAN H "Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions." Türk Doğa ve Fen Dergisi, 12, ss.99 - 103, 2023. 10.46810/tdfd.1233931
ISNAD	Karaderi, Cennet Canan - KAHRAMAN, Hüseyin. "Investigation of Arginine Deiminase Activity in Bacillus cereus and Ralstonia eutropha Under Minimal Conditions". Türk Doğa ve Fen Dergisi 12/2 (2023), 99-103. https://doi.org/10.46810/tdfd.1233931