Biofilm Polysaccharide Display Platform: A Natural, Renewable, and Biocompatible Material for Improved Lipase Performance

Hao Dong, Wenxue Zhang, Yibing Wang, Dong Liu, Ping Wang

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Most of the microorganisms can form biofilms, which makes biofilms an abundant bioresource to be exploited. Due to the limitations of the application of current immobilization methods for biofilms, we developed an immobilization method called the biofilm polysaccharide display (BPD) strategy while maintaining the native biofilm structure and catalytic microenvironment of Clostridium acetobutylicum B3. Lipase Lip181 showed significant improvements in stability after chemical immobilization. For example, immobilized Lip181 retained 74.23% of its original activity after incubation for 14 days, while free Lip181 was totally deactivated. In addition, immobilized Lip181 maintained high residual activity (pH 5.0-11.0), which showed improved resistance to pH changes. Notably, this method did not decrease but slightly increased the relative activity of Lip181 from 6.39 to 6.78 U/mg. Immobilized Lip181 was used to prepare cinnamyl acetate, and it showed a maximum yield of 85.09%. Overall, this biofilm immobilization method may promote the development of biocatalytic and biofilm materials.

Original languageEnglish (US)
Pages (from-to)1373-1381
Number of pages9
JournalJournal of agricultural and food chemistry
Volume68
Issue number5
DOIs
StatePublished - Feb 5 2020

Bibliographical note

Funding Information:
This work was sponsored by the National Natural Science Foundation of China (21636003), the Natural Science Foundation of Shanghai (19ZR1412400), and the Fundamental Research Funds for the Central Universities (22221818014). We would like to thank Editage ( www.editage.cn ) for English language editing.

Publisher Copyright:
© 2020 American Chemical Society.

Keywords

  • Clostridium acetobutylicum
  • biofilm
  • cinnamyl acetate
  • immobilization
  • lipase

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