Production, Isolation, and Purification of L-Asparaginase from Pseudomonas Aeruginosa 50071 Using Solid-state Fermentation

Elbessoumy, Ashraf A; Sarhan, Mohamed S.; Mansour, Jehan

doi:10.5483/bmbrep.2004.37.4.387

Cited by 124 publications

(115 citation statements)

References 21 publications

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“…Molecular weight of asparaginases produced by microorganisms may vary. Molecular weights of L-asparaginase from C. glutamicum, Streptomyces sp.-PDK2 and P. aeruginosa 50079 have been determined as 80 kDa, 140 kDa and 160 kDa respectively by SDS-PAGE [2,6,11]. The present work clearly revealed that maximum production of L-asparaginase from S. albidofl avus could be achieved by cultivating in the medium contain maltose and yeast extract as carbon and nitrogen sources at pH 7.5 and temperature 35°C.…”

Section: Purifi Cation Of the L-asparaginasementioning

confidence: 62%

“…Purity of L-asparaginase was increased up to 99.3-fold with 40% recovery in CM-Sephadex C-50 purifi cation step. L-asparaginase from Pseudomonas aeruginosa 50071 has been purifi ed in CM-Sephadex C-50 column up to 106-fold with 43% yield [11]. L-asparaginase from a marine Streptomyces sp.…”

Section: Purifi Cation Of the L-asparaginasementioning

confidence: 99%

“…The active fractions were collected, dialyzed and concentrated. The purifi ed fraction was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) for the identifi cation of molecular weight of L-asparaginase by using standard proteins [11].…”

Section: Purifi Cation Of L-asparaginasementioning

confidence: 99%

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L-asparaginase production by Streptomyces albidoflavus

2008

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Attempts were made to optimize the cultural conditions for the production of L-asparaginase by Streptomyces albidofl avus under submerged fermentations. Enhanced level of L-asparaginase was found in culture medium supplemented with maltose as carbon source. Yeast extract (2%) was served as good nitrogen source for the production of L-asparaginase. The optimum pH for enzyme production was 7.5 and temperature was 35°C. The release of L-asparaginase from the cells of S. albidofl avus was high when strain was treated with cell disrupting agents like EDTA and lysozyme. The enzyme produced by the strain was purifi ed by ammonium sulfate, Sephadex G-100 and CM-Sephadex C-50 gel fi ltration and the molecular weight was apparently determined as 112 kDa.

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Section: Purifi Cation Of the L-asparaginasementioning

confidence: 62%

Section: Purifi Cation Of the L-asparaginasementioning

confidence: 99%

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L-asparaginase production by Streptomyces albidoflavus

2008

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“…SSF offers many advantages over SmF such as lower energy requirements, less risk of bacterial contamination, less waste water generation and less environmental concerns regarding the disposal of solid waste (Doelle et al, 1992). L-Asparaginase production in SSF has been reported earlier on wheat bran , soya bean meal (Bessoumy et al, 2004) and wastes from three leguminous crops-bran of Cajanus cajan, Phaseolus mungo and Glycine max (Mishra, 2006).…”

mentioning

confidence: 99%

“…This methodology has many disadvantages such as the low concentration product formation and consequent handling, reduction and disposal of large volumes of water during the downstream processing (Bessoumy et al, 2004). Therefore, the SmF methodology is a cost intensive, highly problematic and poorly understood unit operation.…”

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confidence: 99%

Production of Extracellular Anti-leukemic Enzyme L-asparaginase from Fusarium solani AUMC 8615 Grown under Solid-State Fermentation conditions: Purification and Characterization of The Free and Immobilized Enzyme

2016

Egypt. J. Bot.

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OTENTIALITIES of twenty four fungal isolates were investigated for their ability to produce L-asparaginase using modified Czapek's Dox medium. Fusarium solani AUMC 8615 was selected as the most potent fungal strain for the enzyme production under solid state fermentation (SSF) using agro-industrial residues. Wheat bran supported maximum enzyme production followed by rice bran and corn cob. The optimum conditions for maximum production of L-asparaginase under SSF occurred on the fifth day of incubation at 30°C, pH 8.0, 60% of initial moisture content and supplementation with 0.2% (w/v) glucose and 0.5% (w/v) ammonium sulphate. Lasparaginase was purified to homogeneity by ammonium sulphate precipitation, gel filtration and ion exchange chromatography giving 299.58 purification fold. SDS-PAGE showed that the purified enzyme consists of two subunits of molecular weights 70 and 80 kDa, respectively. The enzyme was efficiently immobilized by covalent binding with activated charcoal giving an immobilization yield of 80.40%. Optimum pH values were 9.0 and 8.0 for free and immobilized enzyme, respectively. While, Optimum reaction temperatures were 37°C and 45°C for free and immobilized enzyme, respectively. After incubation for 2 hr at 37°C, the relative activity of free enzyme decreases to 35% whereas for the immobilized enzyme decreased only to 57% at 45°C.

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Sequential optimization and kinetic modeling of L‐asparaginase production by Pectobacteriumcarotovorum in submerged fermentation

Sanjeeviroyar¹,

Rajendran²,

Muthuraj³

et al. 2009

Asia-Pacific J Chem Eng

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L-Asparaginase is a therapeutic enzyme widely used as an antitumor agent for the treatment of acute lymphoblastic leukemia and lymphosarcoma. Its potential applications as a therapeutic agent and food additive require production at high yields in a low-cost medium with high purity and stability. Statistical experimental designs were applied to identify and optimize the significant parameters for the fermentative production of L-asparaginase by Pectobacterium carotovorum Microbial Type Culture Collection (MTCC) 1428. Screening of different carbon sources identified galactose as the best carbon source for the production of L-asparaginase. Twelve medium components were selected and sixteen experiments were carried out based on the Plackett-Burman (PB) design for identifying the most significant medium components. Yeast extract, galactose, monosodium glutamate, MgSO 4 .7H 2 O and CaCl 2 .2H 2 O were found to be the most significant components that affected the production of L-asparaginase, and they were optimized by response surface methodology (RSM) using central composite design. This optimized medium showed maximum production rates of periplasmic and extracellular L-asparaginase of 3.25 and 0.83 U ml −1 , respectively. The periplasmic L-asparaginase production in the optimized medium was twofold higher than in the basal medium. Unstructured kinetic models were applied and satisfactorily described the cell growth, product formation and substrate utilization profile, thus providing a better understanding and prediction of the fermentation profile. This paper details the application of PB experimental design and RSM for the optimization of L-asparaginase production from Pe. carotovorum MTCC 1428 in submerged fermentation. 

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Production, Isolation, and Purification of L-Asparaginase from Pseudomonas Aeruginosa 50071 Using Solid-state Fermentation

Cited by 124 publications

References 21 publications

L-asparaginase production by Streptomyces albidoflavus

L-asparaginase production by Streptomyces albidoflavus

Production of Extracellular Anti-leukemic Enzyme L-asparaginase from Fusarium solani AUMC 8615 Grown under Solid-State Fermentation conditions: Purification and Characterization of The Free and Immobilized Enzyme

Sequential optimization and kinetic modeling of L‐asparaginase production by Pectobacteriumcarotovorum in submerged fermentation

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