Investigation of Arginine deiminase activity in B. cereus and R. eutropha under minimal conditions

Yıl 2023, , 99 - 103, 22.06.2023

Cennet Canan Karaderi , Hüseyin Kahraman

https://doi.org/10.46810/tdfd.1233931

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 Bacillus cereus and R. eutropha in the presence of different minimal sources (Dextrose, Fructose, Glucose, Xylose, Maltose, Nutrient Broth Ramnose, Ribose, Sucrose) under static and shaking (150 rpm) conditions. Arginine deiminase activity was searched. In accordance with conclisions 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 Kelimeler

B. cereus, R. eutropha, arginine deiminase

Proje Numarası

2145

Kaynakça

• 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.
• 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.
• Prajapati B., Supriya N. R. Review on anticancer enzymes and their targeted amino acids, World J Pharm Res, 2017; 6(12), 268-284.
• 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.
• Özalp Erenler Ş. L-asparaginaz geninin (ansB) farklı gram-negatif bakterilere klonlanması, izolasyonu ve ekspresyonu (Doktora tezi). 2007; İnönü Üniversitesi, Fen Bilimleri Enstitüsü, Malatya
• 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.
• Kahraman H., Karaderi C.C., The Importance of Arginine deiminase, Arch Chem and Chem Eng. 2019; 1(1): 1-3.
• 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.
• 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.
• Zou S., Wang X., Liu P., Ke C., Xu S. Arginine metabolism and deprivation in cancer therapy, Biomed Pharm. 2019; 118:1-11.
• 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.
• 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.
• 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.
• Karaderi C.C., Kahraman H. Trehalose Production at Different Mediums in Bacillus cereus and Ralstonia eutropha, Acta Sci Agricul. 2021; 5(10): 2-4.
• 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.
• 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.
• Karaderi, C.C., Bakterilerin Farklı Karbon Kaynaklarının Varlığında Arjinin deiminaz, Trehalaz ve Poli Hidroksi Bütirat Üretiminin Araştırılması (Doktora Tezi), İnönü Üniversitesi, Malatya. 2022.
• Takahara H., Okamoto H., Sugawara K. Enzymatic assay of peptidyl Arginine deiminase, J Biochem. 1986; 99:1417- 1424.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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