Production of a Novel Marine Pseudomonas aeruginosa Recombinant L-Asparaginase: Insight on the Structure and Biochemical Characterization

Qeshmi, Fatemeh Izadpanah; Homaei, Ahmad; Khajeh, Khosro; Kamrani, Ehsan; Fernandes, Pedro

doi:10.1007/s10126-022-10129-9

Cited by 26 publications

(17 citation statements)

References 46 publications

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“…The optimum temperature and pH of partially purified enzyme from P. aeruginosa EWUKR-2 were 37 0 C and 7.5, respectively. These results corresponded with the L-ASNase enzyme from other strains of P. aeruginosa [14,16]. The purification-fold after (NH 4 ) 2 SO 4 precipitation was 2.8 and the yield of concentrated L-ASNase was 101%.…”

Section: Discussionsupporting

confidence: 76%

“…As shown in Fig. 7, the M w of L-ASNase from P. aeruginosa EWUKR-2 was found to be approximately 43 kDa, which was different from the other strains of P. aeruginosa [14][15][16].…”

Section: Discussionmentioning

confidence: 95%

“…L-ASNase can also be used as a model enzyme for the development of new drug delivery systems [9], and as a biosensor for the early detection of leukemia [10]. L-ASNase production has been reported from the bacteria E. coli [4]; the bacteria Aerobacter and Erwinia [11]; the bacteria Serratia and Xanthomonas [12]; the bacteria Pectobacterium and Photobacterium [13]; the strains of Pseudomonas [14][15][16]; the grampositive bacterium Streptomyces and the fungus Aspergillus [11,13]. The purified L-asparaginase enzyme from the bacteria E. coli and Erwinia as well as Serratia marcescens was applied successfully to treat tumor and leukemia [12].…”

Section: Introductionmentioning

confidence: 99%

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Screening and Characterization of L-asparaginase Producing Bacterial Strains from the Soil in Bangladesh

Kabir

Imam²,

Nijhum³

et al. 2022

JAMB

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Although the enzyme L-asparaginase (L-ASNase) from Escherichia coli, Erwinia and Serratia has been applied to treat certain lymphomas and leukemias, several medical complications such as severe immunological responses leading to hypersensitivity, anaphylaxis, etc. have limited its application. The researchers have documented that such impediments are due to the different biochemical and kinetic properties of L-ASNase, which are directly dependent on genetic variations in microbial strains. Thus, there is a compelling need to explore novel L-ASNase producing microorganisms that would exhibit different serological properties while retaining similar and/or better therapeutic effects against cancer cells. Heretofore, L-ASNase producing bacterial strains from Bangladesh have never been isolated and characterized. Therefore, the main objective of this research was to isolate and characterize these strains from unexplored and ecologically different habitats that could lead to developing a potential therapeutic drug with fewer immunological responses and side effects over the existing drugs in order to treat cancer patients in the near future. Two L-ASNase producing bacterial strains were successfully isolated from the soil of Hatirjheel lake in Dhaka for the first time. Molecular characterization revealed that both strains belonged to Pseudomonas aeruginosa and their DNA sequences were submitted to NCBI GenBank. The accession number OK446669 was obtained for the strain of P. aeruginosa EWUKR-1 and OL307081 for P. aeruginosa EWUKR-2. The specific activity of L-ASNase from EWUKR-2 (212.1 ± 14.8 U/mg protein) was significantly higher than that of EWUKR-1 (16.3 ± 0.8 U/mg protein) when they were grown in modified M9 media containing 0.5 g/l glucose at 370C for 24 hours. The experimental results revealed that both of these bacterial strains were extracellular L-ASNase producers. The enzyme from P. aeruginosa EWUKR-2 was partially purified using saturated ammonium sulfate followed by dialysis and concentrated using Vivaspin-20 centrifugal concentrator having MWCO of 30 kDa. The optimum temperature and pH of the partially purified enzyme were 370C and 7.5, respectively. The purification-fold after ammonium sulfate precipitation and yield of the concentrated enzyme were 2.8 and 101%, respectively. SDS-PAGE analysis revealed that the molecular weight of L-ASNase from P. aeruginosa EWUKR-2 was around 43 kDa.

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Section: Discussionsupporting

confidence: 76%

“…As shown in Fig. 7, the M w of L-ASNase from P. aeruginosa EWUKR-2 was found to be approximately 43 kDa, which was different from the other strains of P. aeruginosa [14][15][16].…”

Section: Discussionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

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Screening and Characterization of L-asparaginase Producing Bacterial Strains from the Soil in Bangladesh

Kabir

Imam²,

Nijhum³

et al. 2022

JAMB

View full text Add to dashboard Cite

show abstract

“…The special environment of the ocean may create special enzymes adapted to the industrial environment, such as heat-, salt- and base-tolerant enzymes. The potential of marine enzymes for biotechnology and industrial applications has been shown in numerous studies [ 39 , 40 , 41 , 42 , 43 , 44 , 45 ]. For example, thermostable proteases of marine origin have the potential to be used commercially in protein processing and in the production of protein hydrolysates in the detergent industry [ 46 ].…”

Section: Discussionmentioning

confidence: 99%

Biochemical Characterization and Elucidation of the Hybrid Action Mode of a New Psychrophilic and Cold-Tolerant Alginate Lyase for Efficient Preparation of Alginate Oligosaccharides

Cao

Zhu

et al. 2022

Marine Drugs

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Alginate lyases with unique biochemical properties have irreplaceable value in food and biotechnology industries. Herein, the first new hybrid action mode Thalassotalea algicola-derived alginate lyase gene (TAPL7A) with both psychrophilic and cold-tolerance was cloned and expressed heterologously in E. coli. With the highest sequence identity (43%) to the exolytic alginate lyase AlyA5 obtained from Zobellia galactanivorans, TAPL7A was identified as a new polysaccharide lyases family 7 (PL7) alginate lyase. TAPL7A has broad substrate tolerance with specific activities of 4186.1 U/mg, 2494.8 U/mg, 2314.9 U/mg for polyM, polyG, and sodium alginate, respectively. Biochemical characterization of TAPL7A showed optimal activity at 15 °C, pH 8.0. Interestingly, TAPL7A exhibits both extreme psychrophilic and cold tolerance, which other cold-adapted alginate lyase do not possess. In a wide range of 5–30 °C, the activity can reach 80–100%, and the residual activity of more than 70% can still be maintained after 1 h of incubation. Product analysis showed that TAPL7A adopts a hybrid endo/exo-mode on all three substrates. FPLC and ESI-MS confirmed that the final products of TAPL7A are oligosaccharides with degrees of polymerization (Dps) of 1–2. This study provides excellent alginate lyase candidates for low-temperature environmental applications in food, agriculture, medicine and other industries.

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“…Within the secondary cell wall, xylan is located in‐between cellulose and lignin and plays a major role in maintaining the integrity of cell wall of plants. Structurally, xylan is not a simple polymer, as it is not only composed of homopolymeric or linear backbone but may also contain branches or side chains, which adds heteropolymeric character to its backbone 29,30 . Monomers of β‐D‐xylopyranosyl are linked in a linear fashion to form homopolymeric long chains, whereas addition of variety of side chains such as o‐acetyl, 4‐O‐methyl‐D‐glucurono‐ pyranosyl, α‐L‐arabinofuranosyl, feruloyl or p‐coumaroyl, and so forth contribute to the formation of heteropolymeric structure 29,31,32 …”

Section: Xylan: the Substrate Of Xylanasementioning

confidence: 99%

An insight into microbial sources, classification, and industrial applications of xylanases: A rapid review

Kaur

Joshi

Sharma

et al. 2023

Biotech and App Biochem

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Endo 1,4‐β‐d‐xylanases (EC3.2.1.8) are one of the key lignocellulose hydrolyzing enzymes. Xylan, which is present in copious amounts on earth, forms the primary substrate of endo‐xylanases, which can unchain the constituent monosaccharides linked via β‐1,4‐glycosidic bonds from the xylan backbone. Researchers have shown keen interest in the xylanases belonging to glycoside hydrolase families 10 and 11, whereas those placed in other glycoside hydrolase families are yet to be investigated. Various microbes such as bacteria and fungi harbor these enzymes for the metabolism of their lignocellulose fibers. These microbes can be used as miniature biofactories of xylanase enzymes for a plethora of environmentally benign applications in pulp and paper industry, biofuel production, and for improving the quality of food in bread baking and fruit juice industry. This review highlights the potential of microbes in production of xylanase for industrial biotechnology.

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Production of a Novel Marine Pseudomonas aeruginosa Recombinant L-Asparaginase: Insight on the Structure and Biochemical Characterization

Cited by 26 publications

References 46 publications

Screening and Characterization of L-asparaginase Producing Bacterial Strains from the Soil in Bangladesh

Screening and Characterization of L-asparaginase Producing Bacterial Strains from the Soil in Bangladesh

Biochemical Characterization and Elucidation of the Hybrid Action Mode of a New Psychrophilic and Cold-Tolerant Alginate Lyase for Efficient Preparation of Alginate Oligosaccharides

An insight into microbial sources, classification, and industrial applications of xylanases: A rapid review

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