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• W2896095250 abstract "l-Asparaginase (ASN; EC 3.5.1.1) shows great commercial value because of its ability to reduce toxic levels of acrylamide in foods. To achieve high-efficiency production of l-asparaginase, an open reading frame of 978 bp encoding asparaginase (BcA) was amplified from Bacillus cereus BDRD-ST26, followed by its expression in Bacillus subtilis WB600, with the highest yield of 374.9 U/ml obtained using an amyE-signal peptide. A four-step purification protocol was used to purify BcA, resulting in a 15.1-fold increase in purification yield, with a specific activity of purified BcA at 550.8 U/mg and accompanied by detection of minimal l-glutaminase activity. Maximum BcA activity was detected at 50°C and pH 9.0 in 20 mM Tris–HCl buffer, with a half-life at 50°C of 17.35 min and a Km and kcat of 9.38 mM and 63.6 s−1, respectively. Compared with untreated potato strips, 72% acrylamide (2.35 mg/kg) was removed from potato strips pretreated with BcA. These results indicated that this novel BcA variant represents a potential candidate for application in the food-processing industry." @default.
• W2896095250 created "2018-10-26" @default.
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• W2896095250 date "2019-04-01" @default.
• W2896095250 modified "2023-10-17" @default.
• W2896095250 title "Gene cloning and expression of the l-asparaginase from Bacillus cereus BDRD-ST26 in Bacillus subtilis WB600" @default.
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• W2896095250 doi "https://doi.org/10.1016/j.jbiosc.2018.09.007" @default.
• W2896095250 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30344018" @default.
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