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Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase

The synthesis of a novel α-glucosylated derivative of pterostilbene was performed by a transglycosylation reaction using starch as glucosyl donor, catalyzed by cyclodextrin glucanotransferase (CGTase) from Thermoanaerobacter sp. The reaction was carried out in a buffer containing 20% (v/v) DMSO to e...

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Autores principales: González-Alfonso, José L., Rodrigo-Frutos, David, Belmonte-Reche, Efres, Peñalver, Pablo, Poveda, Ana, Jiménez-Barbero, Jesús, Ballesteros, Antonio O., Hirose, Yoshihiko, Polaina, Julio, Morales, Juan C., Fernández-Lobato, María, Plou, Francisco J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6100302/
https://www.ncbi.nlm.nih.gov/pubmed/29799509
http://dx.doi.org/10.3390/molecules23061271
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author González-Alfonso, José L.
Rodrigo-Frutos, David
Belmonte-Reche, Efres
Peñalver, Pablo
Poveda, Ana
Jiménez-Barbero, Jesús
Ballesteros, Antonio O.
Hirose, Yoshihiko
Polaina, Julio
Morales, Juan C.
Fernández-Lobato, María
Plou, Francisco J.
author_facet González-Alfonso, José L.
Rodrigo-Frutos, David
Belmonte-Reche, Efres
Peñalver, Pablo
Poveda, Ana
Jiménez-Barbero, Jesús
Ballesteros, Antonio O.
Hirose, Yoshihiko
Polaina, Julio
Morales, Juan C.
Fernández-Lobato, María
Plou, Francisco J.
author_sort González-Alfonso, José L.
collection PubMed
description The synthesis of a novel α-glucosylated derivative of pterostilbene was performed by a transglycosylation reaction using starch as glucosyl donor, catalyzed by cyclodextrin glucanotransferase (CGTase) from Thermoanaerobacter sp. The reaction was carried out in a buffer containing 20% (v/v) DMSO to enhance the solubility of pterostilbene. Due to the formation of several polyglucosylated products with CGTase, the yield of monoglucoside was increased by the treatment with a recombinant amyloglucosidase (STA1) from Saccharomyces cerevisiae (var. diastaticus). This enzyme was not able to hydrolyze the linkage between the glucose and pterostilbene. The monoglucoside was isolated and characterized by combining ESI-MS and 2D-NMR methods. Pterostilbene α-d-glucopyranoside is a novel compound. The α-glucosylation of pterostilbene enhanced its solubility in water to approximately 0.1 g/L. The α-glucosylation caused a slight loss of antioxidant activity towards ABTS˙(+) radicals. Pterostilbene α-d-glucopyranoside was less toxic than pterostilbene for human SH-S5Y5 neurons, MRC5 fibroblasts and HT-29 colon cancer cells, and similar for RAW 264.7 macrophages.
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spelling pubmed-61003022018-11-13 Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase González-Alfonso, José L. Rodrigo-Frutos, David Belmonte-Reche, Efres Peñalver, Pablo Poveda, Ana Jiménez-Barbero, Jesús Ballesteros, Antonio O. Hirose, Yoshihiko Polaina, Julio Morales, Juan C. Fernández-Lobato, María Plou, Francisco J. Molecules Article The synthesis of a novel α-glucosylated derivative of pterostilbene was performed by a transglycosylation reaction using starch as glucosyl donor, catalyzed by cyclodextrin glucanotransferase (CGTase) from Thermoanaerobacter sp. The reaction was carried out in a buffer containing 20% (v/v) DMSO to enhance the solubility of pterostilbene. Due to the formation of several polyglucosylated products with CGTase, the yield of monoglucoside was increased by the treatment with a recombinant amyloglucosidase (STA1) from Saccharomyces cerevisiae (var. diastaticus). This enzyme was not able to hydrolyze the linkage between the glucose and pterostilbene. The monoglucoside was isolated and characterized by combining ESI-MS and 2D-NMR methods. Pterostilbene α-d-glucopyranoside is a novel compound. The α-glucosylation of pterostilbene enhanced its solubility in water to approximately 0.1 g/L. The α-glucosylation caused a slight loss of antioxidant activity towards ABTS˙(+) radicals. Pterostilbene α-d-glucopyranoside was less toxic than pterostilbene for human SH-S5Y5 neurons, MRC5 fibroblasts and HT-29 colon cancer cells, and similar for RAW 264.7 macrophages. MDPI 2018-05-25 /pmc/articles/PMC6100302/ /pubmed/29799509 http://dx.doi.org/10.3390/molecules23061271 Text en © 2018 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 Article
González-Alfonso, José L.
Rodrigo-Frutos, David
Belmonte-Reche, Efres
Peñalver, Pablo
Poveda, Ana
Jiménez-Barbero, Jesús
Ballesteros, Antonio O.
Hirose, Yoshihiko
Polaina, Julio
Morales, Juan C.
Fernández-Lobato, María
Plou, Francisco J.
Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase
title Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase
title_full Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase
title_fullStr Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase
title_full_unstemmed Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase
title_short Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase
title_sort enzymatic synthesis of a novel pterostilbene α-glucoside by the combination of cyclodextrin glucanotransferase and amyloglucosidase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6100302/
https://www.ncbi.nlm.nih.gov/pubmed/29799509
http://dx.doi.org/10.3390/molecules23061271
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