Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art

Molecules. 2023 Aug 3;28(15):5848. doi: 10.3390/molecules28155848.

Abstract

As some of the most widely used biocatalysts, lipases have exhibited extreme advantages in many processes, such as esterification, amidation, and transesterification reactions, which causes them to be widely used in food industrial production. However, natural lipases have drawbacks in terms of organic solvent resistance, thermostability, selectivity, etc., which limits some of their applications in the field of foods. In this systematic review, the application of lipases in various food processes was summarized. Moreover, the general structure of lipases is discussed in-depth, and the engineering strategies that can be used in lipase engineering are also summarized. The protocols of some classical methods are compared and discussed, which can provide some information about how to choose methods of lipase engineering. Thermostability engineering and solvent tolerance engineering are highlighted in this review, and the basic principles for improving thermostability and solvent tolerance are summarized. In the future, comput er-aided technology should be more emphasized in the investigation of the mechanisms of reactions catalyzed by lipases and guide the engineering of lipases. The engineering of lipase tunnels to improve the diffusion of substrates is also a promising prospect for further enhanced lipase activity and selectivity.

Keywords: foods; lipases; protein engineering; solvent resistance; thermostability.

Publication types

  • Systematic Review
  • Review

MeSH terms

  • Computers
  • Enzyme Stability
  • Food Industry*
  • Lipase* / chemistry
  • Solvents / chemistry

Substances

  • Lipase
  • Solvents

Grants and funding

This research was financially supported by Jiangsu Funding Program for Excellent Postdoctoral Talent (2023ZB778), Nanjing TECH University Research Startup Funds (No. 39828130).