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Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation

β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environ...

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Autores principales: Mangiagalli, Marco, Lotti, Marina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7832830/
https://www.ncbi.nlm.nih.gov/pubmed/33477853
http://dx.doi.org/10.3390/md19010043
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author Mangiagalli, Marco
Lotti, Marina
author_facet Mangiagalli, Marco
Lotti, Marina
author_sort Mangiagalli, Marco
collection PubMed
description β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic β-galactosidases are broadly studied and employed for biotechnological purposes, the cold-active enzymes are still scarcely explored, although they may prove very useful in biotechnological processes at low temperature. This review covers several issues related to cold-active β-galactosidases, including their classification, structure and molecular mechanisms of cold adaptation. Moreover, their applications are discussed, focusing on the production of lactose-free dairy products as well as on the valorization of cheese whey and the synthesis of glycosyl building blocks for the food, cosmetic and pharmaceutical industries.
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spelling pubmed-78328302021-01-26 Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation Mangiagalli, Marco Lotti, Marina Mar Drugs Review β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic β-galactosidases are broadly studied and employed for biotechnological purposes, the cold-active enzymes are still scarcely explored, although they may prove very useful in biotechnological processes at low temperature. This review covers several issues related to cold-active β-galactosidases, including their classification, structure and molecular mechanisms of cold adaptation. Moreover, their applications are discussed, focusing on the production of lactose-free dairy products as well as on the valorization of cheese whey and the synthesis of glycosyl building blocks for the food, cosmetic and pharmaceutical industries. MDPI 2021-01-19 /pmc/articles/PMC7832830/ /pubmed/33477853 http://dx.doi.org/10.3390/md19010043 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 Review
Mangiagalli, Marco
Lotti, Marina
Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation
title Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation
title_full Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation
title_fullStr Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation
title_full_unstemmed Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation
title_short Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation
title_sort cold-active β-galactosidases: insight into cold adaption mechanisms and biotechnological exploitation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7832830/
https://www.ncbi.nlm.nih.gov/pubmed/33477853
http://dx.doi.org/10.3390/md19010043
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