Arginine deaminase from Pseudomonas aeruginosa PS2: purification, biochemical characterization and in-vitro evaluation of anticancer activity

Bala, Kiran; Husain, Islam; Sharma, Anjana

doi:10.1007/s13205-020-02212-6

Cited by 11 publications

(12 citation statements)

References 42 publications

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“…Free radicals and reactive oxygen species (ROSs) are byproducts of the basal aerobic metabolism of cells. However, excessive generation of ROSs does result in critical oxidative damage to the cellular components of the cells [ 133 , 134 ]. Numerous studies suggest that naringenin exhibits profound antioxidant effects against various oxidative insults, which has been reported to improve cardiac functionality even after injuries [ 135 ].…”

Section: Pharmacological Properties Of Naringeninmentioning

confidence: 99%

Multi-Therapeutic Potential of Naringenin (4′,5,7-Trihydroxyflavonone): Experimental Evidence and Mechanisms

Arafah

Rehman

Mir

et al. 2020

Plants

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Extensive research has been carried out during the last few decades, providing a detailed account of thousands of discovered phytochemicals and their biological activities that have the potential to be exploited for a wide variety of medicinal purposes. These phytochemicals, which are pharmacologically important for clinical use, primarily consist of polyphenols, followed by terpenoids and alkaloids. There are numerous published reports indicating the primary role of phytochemicals proven to possess therapeutic potential against several diseases. However, not all phytochemicals possess significant medicinal properties, and only some of them exhibit viable biological effects. Naringenin, a flavanone found in citrus fruits, is known to improve immunity, repair DNA damage, and scavenge free radicals. Despite the very low bioavailability of naringenin, it is known to exhibit various promising biological properties of medicinal importance, including anti-inflammatory and antioxidant activities. This review focuses on the various aspects related to naringenin, particularly its physicochemical, pharmacokinetic, and pharmacodynamic properties. Furthermore, various pharmacological activities of naringenin, such as anticancer, antidiabetic, hepatoprotective, neuroprotective, cardioprotective, nephroprotective, and gastroprotective effects, have been discussed along with their mechanisms of action.

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Section: Pharmacological Properties Of Naringeninmentioning

confidence: 99%

Multi-Therapeutic Potential of Naringenin (4′,5,7-Trihydroxyflavonone): Experimental Evidence and Mechanisms

Arafah

Rehman

Mir

et al. 2020

Plants

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“…Primarily, the phylogenetic analysis was performed to assess the relatedness of PfADI with ADIs of other species of Pseudomonas genera with established anticancer activities. It was interesting to observe that PfADI clustered with ADI of P. aeruginosa and P. plecoglossicida (which have been previously cloned and expressed in E. coli and have proven anticancer activity in vitro) [29][30][31] and thus encouraged further analysis. Immunogenicity and allergenicity are the major problems associated with the protein therapeutics.…”

Section: Discussionmentioning

confidence: 99%

“…Anticancer ADIs of M. hominis (MhADI) and M. arginini (MaADI) were taken as outgroup species. The phylogenetic tree formed three major clusters (Fig 1) and interestingly, PfADI grouped into cluster I along with the two ADIs (of P. aeruginosa, P. plecoglossicida) with anticancer properties [29][30][31] , thereby anticipating the anticancer potential of PfADI. Further, it may be worthwhile to investigate the ADI of the other related species in cluster I (P. resinovorans, P. putida, P. citronellolis) for potent anticancer activity.…”

Section: Phylogenetic Relatedness Of Pfadimentioning

confidence: 99%

In silico and in vitro analysis of recombinant arginine deiminase from Pseudomonas furukawaii as a potential anticancer enzyme

Dhankhar

Kawatra

Gupta

et al. 2022

Preprint

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Arginine deiminase (ADI), a promising anticancer enzyme from Mycoplasma hominis, is currently in phase III of clinical trials for the treatment of arginine auxotrophic tumors. However, it has been associated with several drawbacks in terms of low stability at human physiological conditions, high immunogenicity, hypersensitivity and systemic toxicity. In our previous work, Pseudomonas furukawaii was identified as a potent producer of ADI with optimum activity under physiological conditions. In the present study, phylogenetic analysis of microbial ADIs indicated P. furukawaii ADI (PfADI) to be closely related to experimentally characterized ADIs of Pseudomonas sp. with proven anticancer activity. Immunoinformatics analysis was performed indicating lower immunogenicity of PfADI than MhADI (M. hominis ADI) both in terms of number of linear and conformational B cell epitopes and T cell epitope density. Overall antigenicity and allergenicity of PfADI was also lower as compared to MhADI, suggesting the applicability of PfADI as an alternative anticancer biotherapeutic. Hence, in vitro experiments were performed in which the ADI coding arcA gene of P. furukawaii was cloned and expressed in E. coli BL21. Recombinant ADI of P. furukawaii was purified, characterized and its anticancer activity was assessed. The enzyme was stable at human physiological conditions (pH 7 and 37 ⁰C) with Km of 1.90 mM. PfADI was found to effectively inhibit the HepG2 cells with an IC50 value of 0.1950 IU/ml. Therefore, the current in silico and in vitro studies establish PfADI as a potential anticancer drug candidate with improved efficacy and low immunogenicity.

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“…Proteolytic tolerance of enzyme was evaluated as described previously with certain modifications (Bala et al, 2020;Husain et al, 2016b). In brief, purified enzyme (0.1 mg/mL) was incubated in 50 mM glycine-HCl buffer (pH 2.5) containing pepsin (0.1 mg/mL, pepsin/enzyme ratio was 1:1 v/v) or 50 mM Tris-HCl buffer containing trypsin (0.1 mg/mL, trypsin/enzyme ratio was 1:1 v/v) for 110 min.…”

Section: Proteolysis Tolerancementioning

confidence: 99%

“…The previously reported yield of bacterial phytases ranged from 12.7% to 21.1% (Choi et al, 2001;Greiner et al, 1993;Hong et al, 2011), which was less as compared with present study (38.56%). Our group is working on bacterial enzymes, and previously we isolated different enzymes from indigenous bacterial strains (Bala et al 2020;Husain et al, 2016aHusain et al, , 2016b. We also isolated indigenous probiotic B. subtilis P6 from poultry soil with excellent phytase-producing ability (Sharma & Trivedi, 2015) and then optimized various process parameters for the maximum yield of phytase (Trivedi et al, 2017).…”

mentioning

confidence: 99%

Purification and characterization of phytase from Bacillus subtilis P6: Evaluation for probiotic potential for possible application in animal feed

2021

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The antinutritional property of phytate is the main problem associated with food animals, but phytase-producing probiotic strain could be the best alternative for resolving this problem. In the present study, phytase from probiotic strain Bacillus subtilis P6 was purified to homogeneity, which showed a relative molecular mass of 40 kDa on native and SDS-PAGE. The purification fold of purified phytase was 86.99, with a specific activity of 104.39 U/mg protein. The purified enzyme showed optimum activity at 40 • C and pH 6.0. Semi-metal ions, such as K + and Ca 2+ , slightly enhance the enzyme activity while Cu 2+ , Co 2+ , and Zn 2+ prominently inhibited phytase activity. Purified phytase showed the highest substrate specificity toward its natural substrate phytate and did not hydrolyze other substrates having a phosphate bond. The purified enzyme exhibited strong proteolytic tolerance against trypsin and pepsin. Further, we evaluated the probiotic potential of B. subtilis and noted that it showed excellent resistance toward high acidic and bile concentrations. Subsequently, it revealed exceptional antimicrobial activity, good hydrophobicity, autoaggregation ability, nonhemolytic, and nonlecithinase activity. Additionally, B. subtilis P6 displayed susceptibility against major antibiotics. Owing to the excellent biochemical properties of phytase with notable probiotic characteristics, B. subtilis P6 may offer the possibility of being a promising candidate for the application in animal feed and food supplements. However, the in vivo use of strain secreting phytase needs to be studied in animals for its intended benefits

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Arginine deaminase from Pseudomonas aeruginosa PS2: purification, biochemical characterization and in-vitro evaluation of anticancer activity

Cited by 11 publications

References 42 publications

Multi-Therapeutic Potential of Naringenin (4′,5,7-Trihydroxyflavonone): Experimental Evidence and Mechanisms

Multi-Therapeutic Potential of Naringenin (4′,5,7-Trihydroxyflavonone): Experimental Evidence and Mechanisms

In silico and in vitro analysis of recombinant arginine deiminase from Pseudomonas furukawaii as a potential anticancer enzyme

Purification and characterization of phytase from Bacillus subtilis P6: Evaluation for probiotic potential for possible application in animal feed

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