Extremophiles Laboratory, Department of Microbiology, School of Biology and Center of Excellence in Phylogeny of Living Organisms, College of Science, University of Tehran, P. O. Box 14155-6455, Tehran, Iran.
Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran.
Mol Biol Rep. 2019 Jun;46(3):3275-3286. doi: 10.1007/s11033-019-04787-7. Epub 2019 Apr 16.
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 RS (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.
已证实几种酶具有抗癌活性。根据癌细胞中氨基酸饥饿的情况,选择了 L-天冬酰胺酶、L-谷氨酰胺酶和 L-精氨酸酶,并在嗜盐菌和耐盐菌中进行了筛选,因为可能患者对嗜盐菌或耐盐菌酶的免疫反应较少。从伊朗不同盐环境中分离并筛选出的 110 株嗜盐菌和耐盐菌中,有些可产生多种抗癌酶。共有 29、4 和 2 株分别产生 L-天冬酰胺酶、L-谷氨酰胺酶和 L-精氨酸酶。根据表型特征和部分 16S rRNA 基因序列分析,阳性菌株——具有产生这些抗癌酶能力的菌株——被鉴定为芽孢杆菌属、迪茨氏菌属、盐单胞菌属、红球菌属、类芽孢杆菌属和片球菌属等革兰氏阳性菌和假单胞菌属、海洋杆菌属、盐单胞菌属、栖海菌属、弧菌属和 Stappia 属等革兰氏阴性菌。抗癌酶的产生主要观察到在杆状革兰氏阴性菌分离物中,尤其是在盐单胞菌属和海洋杆菌属的成员中。大多数酶在生长的静止期产生,在菌株 GBPx3(弧菌属)中 L-天冬酰胺酶的最大酶活为 1.0 IU/ml,在菌株 RS(红球菌属)中 L-谷氨酰胺酶的最大酶活为 0.6 IU/ml,在菌株 GAAy3(片球菌属)中 L-精氨酸酶的最大酶活为 3.1 IU/ml。所选菌株中 L-天冬酰胺酶和 L-谷氨酰胺酶活性的最适温度和 pH 值与人体的生理条件相似,并且这些酶可耐受高达 7.5%浓度的 NaCl。