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Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying

The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. The aim of this study is to encapsulate ADH in mannitol, either with or without additive in order to limit the thermal denaturation of the enzyme during the drying p...

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Detalles Bibliográficos
Autores principales: Shiga, Hirokazu, Joreau, Hiromi, Neoh, Tze Loon, Furuta, Takeshi, Yoshii, Hidefumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3978531/
https://www.ncbi.nlm.nih.gov/pubmed/24662364
http://dx.doi.org/10.3390/pharmaceutics6010185
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author Shiga, Hirokazu
Joreau, Hiromi
Neoh, Tze Loon
Furuta, Takeshi
Yoshii, Hidefumi
author_facet Shiga, Hirokazu
Joreau, Hiromi
Neoh, Tze Loon
Furuta, Takeshi
Yoshii, Hidefumi
author_sort Shiga, Hirokazu
collection PubMed
description The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. The aim of this study is to encapsulate ADH in mannitol, either with or without additive in order to limit the thermal denaturation of the enzyme during the drying process. The retention of ADH activity was investigated at different drying temperatures. When mannitol was used, the encapsulated ADH was found inactive in all the dried powders. This is presumably due to the quick crystallization of mannitol during spray drying that resulted in the impairment of enzyme protection ability in comparison to its amorphous form. Maltodextin (dextrose equivalent = 11) was used to reduce the crystallization of mannitol. The addition of maltodextrin increased ADH activity and drastically changed the powder X-ray diffractogram of the spray-dried powders.
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spelling pubmed-39785312014-04-08 Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying Shiga, Hirokazu Joreau, Hiromi Neoh, Tze Loon Furuta, Takeshi Yoshii, Hidefumi Pharmaceutics Article The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. The aim of this study is to encapsulate ADH in mannitol, either with or without additive in order to limit the thermal denaturation of the enzyme during the drying process. The retention of ADH activity was investigated at different drying temperatures. When mannitol was used, the encapsulated ADH was found inactive in all the dried powders. This is presumably due to the quick crystallization of mannitol during spray drying that resulted in the impairment of enzyme protection ability in comparison to its amorphous form. Maltodextin (dextrose equivalent = 11) was used to reduce the crystallization of mannitol. The addition of maltodextrin increased ADH activity and drastically changed the powder X-ray diffractogram of the spray-dried powders. MDPI 2014-03-24 /pmc/articles/PMC3978531/ /pubmed/24662364 http://dx.doi.org/10.3390/pharmaceutics6010185 Text en © 2014 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 license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Shiga, Hirokazu
Joreau, Hiromi
Neoh, Tze Loon
Furuta, Takeshi
Yoshii, Hidefumi
Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying
title Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying
title_full Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying
title_fullStr Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying
title_full_unstemmed Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying
title_short Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying
title_sort encapsulation of alcohol dehydrogenase in mannitol by spray drying
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3978531/
https://www.ncbi.nlm.nih.gov/pubmed/24662364
http://dx.doi.org/10.3390/pharmaceutics6010185
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