Literature DB >> 30993582

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

Mahdis Zolfaghar1, Mohammad Ali Amoozegar2, Khosro Khajeh3, Hamid Babavalian4, Hamid Tebyanian5.   

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.

Entities:  

Keywords:  Anticancer enzymes; Halophiles; Halophilic; Halotolerant enzymes; L-asparaginase

Mesh:

Substances:

Year:  2019        PMID: 30993582     DOI: 10.1007/s11033-019-04787-7

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.316


  41 in total

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