Purification and characterization of alginate lyase from locally isolated marine<i>Pseudomonas stutzeri</i>MSEA04

Beltagy, Ehab A.; El-Borai, Aliaa M.; Lewiz, Marina; El-Assar, Samy A.

doi:10.1556/018.67.2016.3.8

Cited by 9 publications

(3 citation statements)

References 25 publications

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“…About 55.64 mg of the partially purified L-glutaminase was diluted in 10 ml of 0.1M phosphate buffer at pH 8.0 and purified using Sephadex G-100 gel column (1.6 cm × 50 cm). The elute was obtained at a rate of 0.5 ml/min adjusted with a peristaltic pump and collected in 5 ml (Beltagy et al, 2016;Farag et al, 2021). Protein content and L-glutaminase activity were assessed as previously mentioned.…”

Section: Purification Of L-glutaminasementioning

confidence: 99%

A Highly Purified L-Glutaminase From Immobilized Pseudomonas Sp. Ras123 Cultures With Antitumor and Antibacterial Activities

El-Borai¹,

Sayed

Farag³

et al. 2023

J microb biotech food sci

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L-glutaminase (E.C.3.5.2.1) is an antineoplastic enzyme and in the present study, an extracellular L-glutaminase was produced from a marine local strain identified as Pseudomonas sp. RAS123. The enzyme was produced from free cultures and from cultures immobilized on and in different supports. Pseudomonas sp. RAS123 L-glutaminase produced from immobilized cultures was purified to homogeneity. The specific activity of the enzyme reached 698.655 U/mg protein, with Km and Vmax value of 3.2 mg/ml and 2000 U/ml, respectively. A single band with a molecular weight of about 32.0 kDa was produced by the purified enzyme on SDS-PAGE. Further findings indicated that the pure enzyme's maximum activity occurred at 50°C and pH 9. The enzyme was stable at 60°C for 60 min and in the pH range of 8.0 to 10.0, The effect of chemicals showed that Mn2+, Mg2+, Ni2+ and Fe2+activated the enzyme, while SDS (10% w/v) strongly inhibited the activity of the enzyme. The purified enzyme showed cytotoxic activity against HCT-116, HepG2, MCF-7, HeLa, and CCL-86 cell lines tested with IC50 values of 122, 175, 195, 306, and > 500 µg/ml, respectively. Also, the antibacterial effect of the enzyme showed activity against Staphylococcus aureus, Bacillus subtilis, Streptococcus mutants, Enterobacter cloacae and Escherichia coli. These findings demonstrate that L-glutaminase might be used in numerous biotechnological applications, particularly food and pharmaceutical processing.

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Section: Purification Of L-glutaminasementioning

confidence: 99%

A Highly Purified L-Glutaminase From Immobilized Pseudomonas Sp. Ras123 Cultures With Antitumor and Antibacterial Activities

El-Borai¹,

Sayed

Farag³

et al. 2023

J microb biotech food sci

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“…With the same buffer and a flow rate of 0.5 ml/min, the protein was eluted. The collected fractions of β-mannanase were pooled at 4°C, then protein content and β-mannanase activity were measured (Beltagy et al, 2016;Farag et al, 2018).…”

Section: Gel Filtration Chromatographymentioning

confidence: 99%

Purification and Characterization of a Thermostable β-Mannanase from Halophilic Aspergillus terreus strain ARSA Associated to a Mangrove Plant of Red Sea Coast, Egypt, and its Application in Mannooligosaccharides Production and Juice Clarification

al.¹

2021

Egypt. J. of Aquatic Biolo. and Fish.

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“…Kotil et al (20) found that the better temperature for alginate lyase generation from Pseudomonas aeruginosa AG LSL-11 was 30°C, with activity 0.355 U/ml. Beltagy et al (9), utilized sephadex G-100 in alginate lyase purification from Pseudomonas stutzeri MSEA04 with specific activity 116 U/mg U/mg and yield 48.2%. Table 2.…”

Section: Incubation Temperaturementioning

confidence: 99%

Production, Purification and Inhibition of Alginate Ly-Ase From Local Isolate of Pseudomonas Aeruginosa Na11

Younis¹

2020

Iraqi J. Agric. Sci.

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The point of this study was for determine of the optimum conditions and purification of alginate lyase from local isolate of Pseudomonas aeruginosa NA11, and inhibition of enzyme by various plant extracts. Forty local isolate s of pathogenic Pseudomonas aeruginosa were screened for their ability to produce alginate lyase. Local isolate of P.aeruginosa NA11 showed the maximum efficiency for produce of alginate lyase with high specific activity (14.4 U/mg). Several factors that influence on alginate lyase production from local isolate of P.aeruginosa NA11 were studied, these factors included the type of media, carbon source, nitrogen source, the incubation temperature, pH, and the incubation period. The highest yield of alginate lyase was obtained with the A medium supplemented with 0.5 % of glucose and sodium nitrate at pH 7.5 after 24 hr. incubation at 37 °C. Two chromatographic techniques were used for purification of alginate lyase after precipitation by ammonium sulphate with saturated ratio (0-70 %), including, ion exchange chromatography by DEAE-cellulose and gel filtration by Sephadex G-100. The two steps gave the specific activity of 155.8 U/mg protein, the purification fold was 4.15 and enzymatic yield was 64 %. The molecular weight of partial purified alginate lyase was 57 KDa. The results of antioxidant activity tests for different plants extracts utilizing DPPH radical scavenging activity were showed that the saad extract has high antioxidant activity (71 %) more than other plants extracts. While the results for inhibition experiment of alginate lyase were demonstrated that saad extract was the best inhibitor with inhibition ratio of 86 %.

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Purification and characterization of alginate lyase from locally isolated marinePseudomonas stutzeriMSEA04

Cited by 9 publications

References 25 publications

A Highly Purified L-Glutaminase From Immobilized Pseudomonas Sp. Ras123 Cultures With Antitumor and Antibacterial Activities

A Highly Purified L-Glutaminase From Immobilized Pseudomonas Sp. Ras123 Cultures With Antitumor and Antibacterial Activities

Purification and Characterization of a Thermostable β-Mannanase from Halophilic Aspergillus terreus strain ARSA Associated to a Mangrove Plant of Red Sea Coast, Egypt, and its Application in Mannooligosaccharides Production and Juice Clarification

Production, Purification and Inhibition of Alginate Ly-Ase From Local Isolate of Pseudomonas Aeruginosa Na11

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