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Fragmented ?-Amylase into Microporous Metal-Organic Frameworks as Bioreactors.

ABSTRACT: This work presents an efficient and facile strategy to prepare an ?-amylase bioreactor. As enzymes are quite large to be immobilized inside metal-organic frameworks (MOFs), the tertiary and quaternary structures of ?-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 ?-amylase@MOF bioreactors. Among the different MOFs evaluated, UiO-66 gave the most promising potential due to the size-matching effect of the ?-helix of the fragmented ?-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).

SUBMITTER: Liu LH

PROVIDER: S-EPMC7918099 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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

Liu Li-Hao LH Chiu Ru-Yin RY So Pamela Berilyn PB Lirio Stephen S Huang Hsi-Ya HY Liu Wan-Ling WL Lin Chia-Her CH

Materials (Basel, Switzerland) 20210211 4

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 e ...[more]

PMID: 33670380

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