Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor

A microbioreactor was developed in which selected amine transaminase was immobilized together with the cofactor pyridoxal phosphate (PLP) to allow efficient continuous transamination. The enzyme and cofactor were retained in a porous copolymeric hydrogel matrix formed in a two-plate microreactor wit...

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Auteurs principaux: Tadej Menegatti, Polona Žnidaršič-Plazl
Format: article
Langue:EN
Publié: Frontiers Media S.A. 2021
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Accès en ligne:https://doaj.org/article/07b38756755e45fc942d67603b5f00e3
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spelling oai:doaj.org-article:07b38756755e45fc942d67603b5f00e32021-11-04T04:53:41ZHydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor2296-418510.3389/fbioe.2021.752064https://doaj.org/article/07b38756755e45fc942d67603b5f00e32021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fbioe.2021.752064/fullhttps://doaj.org/toc/2296-4185A microbioreactor was developed in which selected amine transaminase was immobilized together with the cofactor pyridoxal phosphate (PLP) to allow efficient continuous transamination. The enzyme and cofactor were retained in a porous copolymeric hydrogel matrix formed in a two-plate microreactor with an immobilization efficiency of over 97%. After 10 days of continuous operation, 92% of the initial productivity was retained and no leaching of PLP or enzyme from the hydrogel was observed. The microbioreactor with co-immobilized cofactor showed similar performance with and without the addition of exogenous PLP, suggesting that the addition of PLP is not required during the process. The space-time yield of the microbioreactor was 19.91 g L−1 h−1, while the highest achieved biocatalyst productivity was 5.4 mg mgenzyme−1 h−1. The immobilized enzyme also showed better stability over a wider pH and temperature range than the free enzyme. Considering the time and cost efficiency of the immobilization process and the possibility of capacity expansion, such a system is of great potential for industrial application.Tadej MenegattiPolona Žnidaršič-PlazlPolona Žnidaršič-PlazlFrontiers Media S.A.articlecofactor co-immobilizationmicroreaction engineeringflow biocatalysistransaminasehydrogelBiotechnologyTP248.13-248.65ENFrontiers in Bioengineering and Biotechnology, Vol 9 (2021)
institution DOAJ
collection DOAJ
language EN
topic cofactor co-immobilization
microreaction engineering
flow biocatalysis
transaminase
hydrogel
Biotechnology
TP248.13-248.65
spellingShingle cofactor co-immobilization
microreaction engineering
flow biocatalysis
transaminase
hydrogel
Biotechnology
TP248.13-248.65
Tadej Menegatti
Polona Žnidaršič-Plazl
Polona Žnidaršič-Plazl
Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor
description A microbioreactor was developed in which selected amine transaminase was immobilized together with the cofactor pyridoxal phosphate (PLP) to allow efficient continuous transamination. The enzyme and cofactor were retained in a porous copolymeric hydrogel matrix formed in a two-plate microreactor with an immobilization efficiency of over 97%. After 10 days of continuous operation, 92% of the initial productivity was retained and no leaching of PLP or enzyme from the hydrogel was observed. The microbioreactor with co-immobilized cofactor showed similar performance with and without the addition of exogenous PLP, suggesting that the addition of PLP is not required during the process. The space-time yield of the microbioreactor was 19.91 g L−1 h−1, while the highest achieved biocatalyst productivity was 5.4 mg mgenzyme−1 h−1. The immobilized enzyme also showed better stability over a wider pH and temperature range than the free enzyme. Considering the time and cost efficiency of the immobilization process and the possibility of capacity expansion, such a system is of great potential for industrial application.
format article
author Tadej Menegatti
Polona Žnidaršič-Plazl
Polona Žnidaršič-Plazl
author_facet Tadej Menegatti
Polona Žnidaršič-Plazl
Polona Žnidaršič-Plazl
author_sort Tadej Menegatti
title Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor
title_short Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor
title_full Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor
title_fullStr Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor
title_full_unstemmed Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor
title_sort hydrogel-based enzyme and cofactor co-immobilization for efficient continuous transamination in a microbioreactor
publisher Frontiers Media S.A.
publishDate 2021
url https://doaj.org/article/07b38756755e45fc942d67603b5f00e3
work_keys_str_mv AT tadejmenegatti hydrogelbasedenzymeandcofactorcoimmobilizationforefficientcontinuoustransaminationinamicrobioreactor
AT polonaznidarsicplazl hydrogelbasedenzymeandcofactorcoimmobilizationforefficientcontinuoustransaminationinamicrobioreactor
AT polonaznidarsicplazl hydrogelbasedenzymeandcofactorcoimmobilizationforefficientcontinuoustransaminationinamicrobioreactor
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