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Isolation and screening of extracellular anticancer enzymes from halophilic and halotolerant bacteria from different saline environments in Iran
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 halophili...
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Published in: | Molecular biology reports 2019-06, Vol.46 (3), p.3275-3286 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 R
2
S
25
(
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. |
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ISSN: | 0301-4851 1573-4978 |
DOI: | 10.1007/s11033-019-04787-7 |