Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors

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, dithiothreitol (DTT), and...

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Detalles Bibliográficos
Autores principales: Liu, Li-Hao, Chiu, Ru-Yin, So, Pamela Berilyn, Lirio, Stephen, Huang, Hsi-Ya, Liu, Wan-Ling, Lin, Chia-Her
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7918099/
https://www.ncbi.nlm.nih.gov/pubmed/33670380
http://dx.doi.org/10.3390/ma14040870
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author Liu, Li-Hao
Chiu, Ru-Yin
So, Pamela Berilyn
Lirio, Stephen
Huang, Hsi-Ya
Liu, Wan-Ling
Lin, Chia-Her
author_facet Liu, Li-Hao
Chiu, Ru-Yin
So, Pamela Berilyn
Lirio, Stephen
Huang, Hsi-Ya
Liu, Wan-Ling
Lin, Chia-Her
author_sort Liu, Li-Hao
collection PubMed
description 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, dithiothreitol (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).
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spelling pubmed-79180992021-03-02 Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors Liu, Li-Hao Chiu, Ru-Yin So, Pamela Berilyn Lirio, Stephen Huang, Hsi-Ya Liu, Wan-Ling Lin, Chia-Her Materials (Basel) Article 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, dithiothreitol (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). MDPI 2021-02-11 /pmc/articles/PMC7918099/ /pubmed/33670380 http://dx.doi.org/10.3390/ma14040870 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Liu, Li-Hao
Chiu, Ru-Yin
So, Pamela Berilyn
Lirio, Stephen
Huang, Hsi-Ya
Liu, Wan-Ling
Lin, Chia-Her
Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors
title Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors
title_full Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors
title_fullStr Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors
title_full_unstemmed Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors
title_short Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors
title_sort fragmented α-amylase into microporous metal-organic frameworks as bioreactors
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7918099/
https://www.ncbi.nlm.nih.gov/pubmed/33670380
http://dx.doi.org/10.3390/ma14040870
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