Fragmented α-amylase into microporous metal-organic frameworks as bioreactors

Li Hao Liu, Ru Yin Chiu, Pamela Berilyn So, Stephen Lirio, Hsi Ya Huang, Wan Ling Liu, Chia Her Lin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


This work presents an efficient and facile strategy to prepare an α-amylase bioreactor. As enzymes are quite large to be immobilized inside metal-organic frameworks (MOFs), the tertiary and quaternary structures of α-amylase were first disrupted using a combination of urea, dithio-threitol (DTT), and iodoacetamide (IAA). After losing its tertiary structure, the unfolded proteins can now penetrate into the microporous MOFs, affording fragmented α-amylase@MOF bioreactors. Among the different MOFs evaluated, UiO-66 gave the most promising potential due to the size-matching effect of the α-helix of the fragmented α-amylase with the pore size of UiO-66. The prepared bioreactor exhibited high yields of small carbohydrate (maltose) even when reused up to 15 times (>80% conversion).

Original languageEnglish
Article number870
Pages (from-to)1-8
Number of pages8
Issue number4
Publication statusPublished - 2021 Feb 2


  • Bioreactor
  • Catalysis
  • Enzyme immobilization
  • Metal-organic framework
  • Size matching

ASJC Scopus subject areas

  • General Materials Science


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