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

doi:10.3390/ma14040870

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

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

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 language	English
Article number	870
Pages (from-to)	1-8
Number of pages	8
Journal	Materials
Volume	14
Issue number	4
DOIs	https://doi.org/10.3390/ma14040870
Publication status	Published - 2021 Feb 2

Keywords

Bioreactor
Catalysis
Enzyme immobilization
Metal-organic framework
Size matching

ASJC Scopus subject areas

General Materials Science

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10.3390/ma14040870

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title = "Fragmented α-amylase into microporous metal-organic frameworks as bioreactors",

abstract = "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).",

keywords = "Bioreactor, Catalysis, Enzyme immobilization, Metal-organic framework, Size matching",

author = "Liu, \{Li Hao\} and Chiu, \{Ru Yin\} and So, \{Pamela Berilyn\} and Stephen Lirio and Huang, \{Hsi Ya\} and Liu, \{Wan Ling\} and Lin, \{Chia Her\}",

note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",

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T1 - Fragmented α-amylase into microporous metal-organic frameworks as bioreactors

AU - Liu, Li Hao

AU - Chiu, Ru Yin

AU - So, Pamela Berilyn

AU - Lirio, Stephen

AU - Huang, Hsi Ya

AU - Liu, Wan Ling

AU - Lin, Chia Her

PY - 2021/2/2

Y1 - 2021/2/2

N2 - 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).

AB - 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).

KW - Bioreactor

KW - Catalysis

KW - Enzyme immobilization

KW - Metal-organic framework

KW - Size matching

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UR - https://www.scopus.com/pages/publications/85100918125#tab=citedBy

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DO - 10.3390/ma14040870

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SN - 1996-1944

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JO - Materials

JF - Materials

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M1 - 870

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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