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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Farahat MG,Amr D,Galal Adoi
10.1016/j.ijbiomac.2019.10.258subject
Has Abstractpub_date
2020-01-15 00:00:00pages
685-695eissn
0141-8130issn
1879-0003pii
S0141-8130(19)35196-7journal_volume
143pub_type
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