Reduction of acrylamide level through blanching with treatment by an extremely thermostable l-asparaginase during French fries processing

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.

Antitumor activity and ability to prevent acrylamide formation in fried foods of asparaginase from soybean root nodules

“…chrysanthemi 3,937 (118.7 U/mg) (Kotzia & Labrou, ), Aquabacterium sp . A7‐Y (458.9 U/mg) (Sun et al, ), Streptomyces thermoluteus (68.3 U/mg) and S. griseus (48.9 U/mg) (Hatanaka et al, ), but it is lower than the specific activity of the archaea L‐asparaginases (Chohan & Rashid, ; Zuo, Zhang, Jiang, & Mu, ). The enzyme activity of srnASNase toward L‐asparagine was considered as 100%.…”

Design of a high‐efficiency synthetic system for l‐asparaginase production in Bacillus subtilis

“…After decades of research, Escherichia coli and Erwinia chrysanthemi l ‐asparaginases have been used as effective antitumor drugs for the treatment of pediatric acute lymphoblastic leukemia . In the food industry, l ‐asparaginase has been used to reduce carcinogenic acrylamide levels . However, the low yield of l ‐asparaginase has restricted the application of this enzyme in the food and pharmaceutical industries.…”

“…After decades of research, Escherichia coli and Erwinia chrysanthemi L-asparaginases have been used as effective antitumor drugs for the Abbreviations: CDW, cells dry weight; DO, dissolved oxygen; pyasnaseMut, a high yield mutant of Pyrococcus yayanosii CH1 Lasparaginase which was construct by our previous works; qPCR, quantitative real time PCR treatment of pediatric acute lymphoblastic leukemia [4,5]. In the food industry, L-asparaginase has been used to reduce carcinogenic acrylamide levels [6][7][8]. However, the low yield of L-asparaginase has restricted the application of this enzyme in the food and pharmaceutical industries.…”

Process‐centric and data‐centric strategies for enhanced production of l‐asparaginase—an anticancer enzyme, using marine‐derived Aspergillus niger

“…In the food industry, LAs from Aspergillus niger and Aspergillus oryzae were used for reducing acrylamide formation. The enzyme (from Escherichia coli and Erwinia chrysanthemi ) has been in use in the field of medicine for over 40 years as an effective antitumor drug especially for pediatric acute lymphoblastic leukemia . However, there are certain issues involved with commercially available LA.…”