Characterization of a novel type I L-asparaginase from Acinetobacter soli and its ability to inhibit acrylamide formation in potato chips

Linshu Jiao, Huibing Chi, Zhaoxin Lu, Chong Zhang, Shir Reen Chia, Pau Loke Show, Yang Tao, Fengxia Lu

Research output: Contribution to journalArticlepeer-review

47 Scopus citations

Abstract

L-Asparaginases have the potential to inhibit the formation of acrylamide, a harmful toxin formed during high temperature processing of food. A novel bacterium which produces L-asparaginase was screened. Type I L-asparaginase gene from Acinetobacter soli was cloned and expressed in Escherichia coli. The recombinant L-asparaginase had an activity of 42.0 IU mL−1 and showed no activity toward L-glutamine and D-asparagine. The recombinant L-asparaginase exhibited maximum catalytic activity at pH 8.0 and 40°C. The enzyme was stable in the pH ranging from 6.0 to 9.0. The activity of the recombinant enzyme was substantially enhanced by Ba2+, dithiothreitol, and β-mercaptoethanol. The Km and Vmax values of the L-asparaginase for the L-asparagine were 3.22 mmol L−1 and 1.55 IU μg−1, respectively. Moreover, the recombinant L-asparaginase had the ability to mitigate acrylamide formation in potato chips. Compared with the untreated group, the content of acrylamide in samples treated with the enzyme was effectively decreased by 55.9%. These results indicate that the novel type I L-asparaginase has the potential for application in the food processing industry.

Original languageBritish English
Pages (from-to)672-678
Number of pages7
JournalJournal of Bioscience and Bioengineering
Volume129
Issue number6
DOIs
StatePublished - Jun 2020

Keywords

  • Acinetobacter soli
  • Acrylamide inhibition
  • Characterization
  • Heterologous expression
  • L-Asparaginase

Fingerprint

Dive into the research topics of 'Characterization of a novel type I L-asparaginase from Acinetobacter soli and its ability to inhibit acrylamide formation in potato chips'. Together they form a unique fingerprint.

Cite this