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Jia, Mingmei; Xu, Meijuan; He, Beibei; Rao, Zhiming
Journal of agricultural and food chemistry, 10/2013, Letnik: 61, Številka: 39Journal Article
This study focused on the cloning, overexpression, and characterization of the gene encoding l-asparaginase (ansZ) from a nonpathogenic strain of Bacillus subtilis B11–06. The recombinant enzyme showed high thermostability and low affinity to l-glutamine. The ansZ gene, encoding a putative l-asparaginase II, was amplified by PCR and expressed in B. subtilis 168 using the shuttle vector pMA5. The activity of the recombinant enzyme was 9.98 U/mL, which was significantly higher than that of B. subtilis B11–06. The recombinant enzyme was purified by a two-step procedure including ammonium sulfate fractionation and hydrophobic interaction chromatography. The optimum pH and temperature of the recombinant enzyme were 7.5 and 40 °C, respectively. The enzyme was quite stable at a pH range of 6.0–9.0 and exhibited about 14.7 and 9.0% retention of activity following 2 h incubation at 50 or 60 °C, respectively. The K m for l-asparagine was 0.43 mM, and the V max was 77.51 μM/min. Results of this study also revealed the potential industrial application of this enzyme in reducing acrylamide formation during the potato frying process.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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