| Autor: |
Annsy Arredondo-Nuñez, Gisele Monteiro, Carol N. Flores-Fernández, Lina Antenucci, Perttu Permi, Amparo Iris Zavaleta |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
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| Zdroj: |
Life, Vol 13, Iss 11, p 2145 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2075-1729 |
| DOI: |
10.3390/life13112145 |
| Popis: |
L-asparaginases from bacterial sources have been used in antineoplastic treatments and the food industry. A type II L-asparaginase encoded by the N-truncated gene ansZP21 of halotolerant Bacillus subtilis CH11 isolated from Chilca salterns in Peru was expressed using a heterologous system in Escherichia coli BL21 (DE3)pLysS. The recombinant protein was purified using one-step nickel affinity chromatography and exhibited an activity of 234.38 U mg−1 and a maximum catalytic activity at pH 9.0 and 60 °C. The enzyme showed a homotetrameric form with an estimated molecular weight of 155 kDa through gel filtration chromatography. The enzyme half-life at 60 °C was 3 h 48 min, and L-asparaginase retained 50% of its initial activity for 24 h at 37 °C. The activity was considerably enhanced by KCl, CaCl2, MgCl2, mercaptoethanol, and DL-dithiothreitol (p-value < 0.01). Moreover, the Vmax and Km were 145.2 µmol mL−1 min−1 and 4.75 mM, respectively. These findings evidence a promising novel type II L-asparaginase for future industrial applications. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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