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Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3
The transformation of ginsenoside Rb1 into a specific minor ginsenoside using Aspergillus niger KCCM 11239, as well as the identification of the transformed products and the pathway via thin layer chromatography and high performance liquid chromatography were evaluated to develop a new biologically...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3915331/ https://www.ncbi.nlm.nih.gov/pubmed/24558310 http://dx.doi.org/10.1016/j.jgr.2013.11.008 |
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author | Chang, Kyung Hoon Jo, Mi Na Kim, Kee-Tae Paik, Hyun-Dong |
author_facet | Chang, Kyung Hoon Jo, Mi Na Kim, Kee-Tae Paik, Hyun-Dong |
author_sort | Chang, Kyung Hoon |
collection | PubMed |
description | The transformation of ginsenoside Rb1 into a specific minor ginsenoside using Aspergillus niger KCCM 11239, as well as the identification of the transformed products and the pathway via thin layer chromatography and high performance liquid chromatography were evaluated to develop a new biologically active material. The conversion of ginsenoside Rb1 generated Rd, Rg3, Rh2, and compound K although the reaction rates were low due to the low concentration. In enzymatic conversion, all of the ginsenoside Rb1 was converted to ginsenoside Rd and ginsenoside Rg3 after 24 h of incubation. The crude enzyme (β-glucosidase) from A. niger KCCM 11239 hydrolyzed the β-(1→6)-glucosidic linkage at the C-20 of ginsenoside Rb1 to generate ginsenoside Rd and ginsenoside Rg3. Our experimental demonstration showing that A. niger KCCM 11239 produces the ginsenoside-hydrolyzing β-glucosidase reflects the feasibility of developing a specific bioconversion process to obtain active minor ginsenosides. |
format | Online Article Text |
id | pubmed-3915331 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
record_format | MEDLINE/PubMed |
spelling | pubmed-39153312014-02-20 Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3 Chang, Kyung Hoon Jo, Mi Na Kim, Kee-Tae Paik, Hyun-Dong J Ginseng Res Research Article The transformation of ginsenoside Rb1 into a specific minor ginsenoside using Aspergillus niger KCCM 11239, as well as the identification of the transformed products and the pathway via thin layer chromatography and high performance liquid chromatography were evaluated to develop a new biologically active material. The conversion of ginsenoside Rb1 generated Rd, Rg3, Rh2, and compound K although the reaction rates were low due to the low concentration. In enzymatic conversion, all of the ginsenoside Rb1 was converted to ginsenoside Rd and ginsenoside Rg3 after 24 h of incubation. The crude enzyme (β-glucosidase) from A. niger KCCM 11239 hydrolyzed the β-(1→6)-glucosidic linkage at the C-20 of ginsenoside Rb1 to generate ginsenoside Rd and ginsenoside Rg3. Our experimental demonstration showing that A. niger KCCM 11239 produces the ginsenoside-hydrolyzing β-glucosidase reflects the feasibility of developing a specific bioconversion process to obtain active minor ginsenosides. 2013-12-13 2014-01 /pmc/articles/PMC3915331/ /pubmed/24558310 http://dx.doi.org/10.1016/j.jgr.2013.11.008 Text en © 2014 The Korean Society of Ginseng. Published by Elsevier B.V. All rights reserved. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Chang, Kyung Hoon Jo, Mi Na Kim, Kee-Tae Paik, Hyun-Dong Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3 |
title | Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3 |
title_full | Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3 |
title_fullStr | Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3 |
title_full_unstemmed | Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3 |
title_short | Evaluation of glucosidases of Aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside Rb1 to ginsenosides Rg3 |
title_sort | evaluation of glucosidases of aspergillus niger strain comparing with other glucosidases in transformation of ginsenoside rb1 to ginsenosides rg3 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3915331/ https://www.ncbi.nlm.nih.gov/pubmed/24558310 http://dx.doi.org/10.1016/j.jgr.2013.11.008 |
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