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Isolation and screening of extracellular anticancer enzymes from halophilic and halotolerant bacteria from different saline environments in Iran

  • Mahdis Zolfaghar
  • Mohammad Ali AmoozegarEmail author
  • Khosro Khajeh
  • Hamid Babavalian
  • Hamid Tebyanian
Original Article

Abstract

It was confirmed that several enzymes have anti-cancer activity. The enzymes l-asparaginase, l-glutaminase, and l-arginase were chosen according to amino acids starvation in cancer cells and screened in halophilic and halotolerant bacteria, given probably less immunological reactions of halophilic or halotolerant enzymes in patients. Out of 110 halophilic and halotolerant strains, isolated from different saline environments in Iran and screened, some could produce a variety of anticancer enzymes. A total of 29, 4, and 2 strains produced l-asparaginase, l-glutaminase, and l-arginase, respectively. According to the phenotypic characteristics and partial 16S rRNA gene sequence analysis, the positive strains—strains with the ability to produce these anticancer enzymes—were identified as the members of the genera: Bacillus, Dietzia, Halobacillus, Rhodococcus, Paenibacillus and Planococcus as Gram-positive bacteria and Pseudomonas, Marinobacter, Halomonas, Idiomarina, Vibrio and Stappia as Gram-negative bacteria. The production of anticancer enzymes was mostly observed in the rod-shaped Gram-negative isolates, particularly in the members of the genera Halomonas and Marinobacter. Most of the enzymes were produced in the stationary phase of growth and the maximum enzyme activity was experienced in strain GBPx3 (Vibrio sp.) for l-asparaginase at 1.0 IU/ml, strain R2S25 (Rhodococcus sp.) for l-glutaminase at 0.6 IU/ml and strain GAAy3 (Planococcus sp.) for l-arginase at 3.1 IU/ml. The optimum temperature and pH for l-asparaginase and l-glutaminase activities in selected strains were similar to the physiological conditions of human body and the enzymes could tolerate NaCl up to 7.5% concentration.

Keywords

Anticancer enzymes Halophiles l-asparaginase Halophilic Halotolerant enzymes 

Notes

Acknowledgements

This work was supported by a Grant from the Research Council of University of Tehran.

Compliance with ethical standards

Conflict of interest

There is no conflict of interest.

Supplementary material

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Supplementary material 1 (DOCX 23 kb)
11033_2019_4787_MOESM2_ESM.jpg (76 kb)
Supplementary material 2 (JPEG 76 kb)
11033_2019_4787_MOESM3_ESM.jpg (54 kb)
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Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Extremophiles Laboratory, Department of Microbiology, School of Biology and Center of Excellence in Phylogeny of Living Organisms, College of ScienceUniversity of TehranTehranIran
  2. 2.Department of Biochemistry, Faculty of Biological ScienceTarbiat Modares UniversityTehranIran
  3. 3.Applied Virology Research CenterBaqiyatallah University of Medical SciencesTehranIran
  4. 4.Research Center for Prevention of Oral and Dental DiseasesBaqiyatallah University of Medical SciencesTehranIran

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