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  • Title: Reduction of acrylamide level through blanching with treatment by an extremely thermostable L-asparaginase during French fries processing.
    Author: Zuo S, Zhang T, Jiang B, Mu W.
    Journal: Extremophiles; 2015 Jul; 19(4):841-51. PubMed ID: 26077968.
    Abstract:
    Bacterial L-asparaginase catalyzes the hydrolysis of L-asparagine to L-aspartic acid. It is normally used as an antineoplastic drug applied in lymphoblastic leukemia chemotherapy and as a food processing aid in baked or fried food industry to inhibit the formation of acrylamide. The present study demonstrates cloning, expression, and characterization of a thermostable L-asparaginase from Thermococcus zilligii AN1 TziAN1_1 and also evaluates the potential for enzymatic acrylamide mitigation in French fries using this enzyme. The recombinant L-asparaginase was purified to homogeneity by nickel-affinity chromatography. The purified enzyme displayed the maximum activity at pH 8.5 and 90 °C, and the optimum temperature was the highest ever reported. The K m, k cat, and k cat/K m values toward L-asparagine were measured to be 6.08 mM, 3267 s(-1), and 537.3 mM(-1) s(-1), respectively. The enzyme retained 70 % of its original activity after 2 h of incubation at 85 °C. When potato samples were treated with 10 U/mL of L-asparaginase at 80 °C for only 4 min, the acrylamide content in final French fries was reduced by 80.5 % compared with the untreated control. Results of this study revealed that the enzyme was highly active at elevated temperatures, reflecting the potential of the T. zilligii L-asparaginase in the food processing industry.
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