SpyCatcher/SpyTag-Mediated Self-Assembly of a Supramolecular Complex for Improved Biocatalytic Production of Trehalose

X. Shen, S. Tang, Q. Xu, H. Huang, L. Jiang

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Trehalose has been utilized in the food, cosmetic, and pharmaceutical industries due to its ability to stabilize biomolecules. In this study, we developed a strategy of constructing a self-assembling supramolecular multienzyme complex for the production of trehalose using SpyCatcher and SpyTag. Maltooligosyl trehalose synthase (MTS) and maltooligosyl trehalose trehalohydrolase (MTH) were fused to SpyCatcher and its corresponding ligand, SpyTag. The fused MTS-SpyCatcher (MTS-SC) and MTH-SpyTag (MTH-ST) self-assembled into a supramolecular multienzyme complex (MTS-MTH) via the isopeptide bonds formed between SpyCatcher and SpyTag. MTS-MTH showed the faster reaction rate, which reached the peak of trehalose conversion rate 10 h earlier than the free enzymes. The results demonstrate that the multienzyme self-assembly via the protein-peptide interactions of SpyCatcher and SpyTag can increase the catalytic efficiency of sequential reactions.

Original languageEnglish
Pages (from-to)596-602
Number of pages7
JournalApplied Biochemistry and Microbiology
Volume55
Issue number6
DOIs
StatePublished - 1 Nov 2019

Keywords

  • SpyCatcher
  • SpyTag
  • maltooligosyl trehalose synthase
  • maltooligosyl trehalose trehalohydrolase
  • multienzyme self-assembly
  • trehalose

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