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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Tadej Menegatti, Polona Žnidaršič-Plazl
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	cofactor co-immobilization microreaction engineering flow biocatalysis transaminase hydrogel Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/07b38756755e45fc942d67603b5f00e3
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:07b38756755e45fc942d67603b5f00e3
record_format	dspace
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
_version_	1718445191167213568

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

Ejemplares similares