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Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis
Platycosides, Platycodi radix (Platycodon grandiflorus root) saponins, are used as food supplements and exert diverse pharmacological activities. Deglycosylation of saponins enhances their biological efficacy, and deglycosylated platycosides are produced mainly through enzymatic hydrolysis. However,...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Korean Society for Microbiology and Biotechnology
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9628805/ https://www.ncbi.nlm.nih.gov/pubmed/35283429 http://dx.doi.org/10.4014/jmb.2112.12020 |
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author | Shin, Kyung-Chul Kil, Tae-Geun Kang, Su-Hwan Oh, Deok-Kun |
author_facet | Shin, Kyung-Chul Kil, Tae-Geun Kang, Su-Hwan Oh, Deok-Kun |
author_sort | Shin, Kyung-Chul |
collection | PubMed |
description | Platycosides, Platycodi radix (Platycodon grandiflorus root) saponins, are used as food supplements and exert diverse pharmacological activities. Deglycosylation of saponins enhances their biological efficacy, and deglycosylated platycosides are produced mainly through enzymatic hydrolysis. However, the types of available deglycosylated platycosides remain limited because of a lack of hydrolyzing enzymes that can act on specific glycosides in glycosylated platycosides. In this study, a crude enzyme from Aspergillus tubingensis converted platycoside E (PE) and polygalacin D(3) (PGD3) into deglucose-apiose-xylosylated (deGAX)-platycodin D (PD) and deGAX-polygalacin D (PGD), respectively. The products were identified through LC/MS analysis by specifically hydrolyzing all glucose residues at C-3, and apiose and xylose residues at C-28 of platycoside. The hydrolytic activity of the crude enzyme obtained after the cultivation of the fungus using citrus pectin and corn steep solid as carbon and nitrogen sources, respectively, in culture medium was increased compared with those using other carbon and nitrogen sources. The crude enzyme from A. tubingensis was the most effective in producing deGAX platycoside at pH 5.0 and 60°C. The crude enzyme produced 0.32 mg/ml deGAX-PD and 0.34 mg/ml deGAX-PGD from 1 mg/ml PE and 1 mg/ml PGD3 (at pH 5.0 and 60°C) for 12 and 10 h, with productivities of 32.0 and 42.5 mg/l/h and molar yields of 62.1 and 59.6%, respectively. To the best of our knowledge, this is the first study to produce deGAX platycosides from glycosylated platycosides. |
format | Online Article Text |
id | pubmed-9628805 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Korean Society for Microbiology and Biotechnology |
record_format | MEDLINE/PubMed |
spelling | pubmed-96288052022-12-13 Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis Shin, Kyung-Chul Kil, Tae-Geun Kang, Su-Hwan Oh, Deok-Kun J Microbiol Biotechnol Research article Platycosides, Platycodi radix (Platycodon grandiflorus root) saponins, are used as food supplements and exert diverse pharmacological activities. Deglycosylation of saponins enhances their biological efficacy, and deglycosylated platycosides are produced mainly through enzymatic hydrolysis. However, the types of available deglycosylated platycosides remain limited because of a lack of hydrolyzing enzymes that can act on specific glycosides in glycosylated platycosides. In this study, a crude enzyme from Aspergillus tubingensis converted platycoside E (PE) and polygalacin D(3) (PGD3) into deglucose-apiose-xylosylated (deGAX)-platycodin D (PD) and deGAX-polygalacin D (PGD), respectively. The products were identified through LC/MS analysis by specifically hydrolyzing all glucose residues at C-3, and apiose and xylose residues at C-28 of platycoside. The hydrolytic activity of the crude enzyme obtained after the cultivation of the fungus using citrus pectin and corn steep solid as carbon and nitrogen sources, respectively, in culture medium was increased compared with those using other carbon and nitrogen sources. The crude enzyme from A. tubingensis was the most effective in producing deGAX platycoside at pH 5.0 and 60°C. The crude enzyme produced 0.32 mg/ml deGAX-PD and 0.34 mg/ml deGAX-PGD from 1 mg/ml PE and 1 mg/ml PGD3 (at pH 5.0 and 60°C) for 12 and 10 h, with productivities of 32.0 and 42.5 mg/l/h and molar yields of 62.1 and 59.6%, respectively. To the best of our knowledge, this is the first study to produce deGAX platycosides from glycosylated platycosides. The Korean Society for Microbiology and Biotechnology 2022-04-28 2022-02-17 /pmc/articles/PMC9628805/ /pubmed/35283429 http://dx.doi.org/10.4014/jmb.2112.12020 Text en Copyright © 2022 by the authors. Licensee KMB. https://creativecommons.org/licenses/by/4.0/This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Research article Shin, Kyung-Chul Kil, Tae-Geun Kang, Su-Hwan Oh, Deok-Kun Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis |
title | Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis |
title_full | Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis |
title_fullStr | Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis |
title_full_unstemmed | Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis |
title_short | Production of Deglucose-Apiose-Xylosylated Platycosides from Glycosylated Platycosides by Crude Enzyme from Aspergillus tubingensis |
title_sort | production of deglucose-apiose-xylosylated platycosides from glycosylated platycosides by crude enzyme from aspergillus tubingensis |
topic | Research article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9628805/ https://www.ncbi.nlm.nih.gov/pubmed/35283429 http://dx.doi.org/10.4014/jmb.2112.12020 |
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