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  • Title: Molecular cloning, structural modeling and characterization of a novel glutaminase-free L-asparaginase from Cobetia amphilecti AMI6.
    Author: Farahat MG, Amr D, Galal A.
    Journal: Int J Biol Macromol; 2020 Jan 15; 143():685-695. PubMed ID: 31759010.
    Abstract:
    The exploration of new sources of L-asparaginase with low glutaminase activity is of great interest in both medical and food applications. In the current study, a novel L-asparaginase gene (CobAsnase) from halotolerant Cobetia amphilecti AMI6 was cloned and over-expressed in Escherichia coli. The enzyme had a molecular mass of 37 kDa on SDS-PAGE and dynamic light scattering (DLS) analysis revealed that CobAsnase is a homotetramer in solution. The purified enzyme showed optimum activity at pH and temperature of 7 and 60 °C, respectively, with obvious thermal stability. It exhibited strict substrate specificity towards L-asparagine with no detectable activity on L-glutamine. Pre-treatment of potato slices by CobAsnase prior to frying reduced the acrylamide contents in the processed chips up to 81% compared with untreated control. These results suggest that CobAsnase is a potential candidate for applications in the food industry for mitigation of acrylamide formation in fried potato and baked foods.
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