Cargando…

Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi

In the present work, we reported the enzymatic preparation of deapio-platycodin D (dPD) and platycodin D (PD) optimized by response surface methodology (RSM) from Radix Platycodi. During investigation of the hydrolysis of crude platycosides by various glycoside hydrolases, snailase showed a strong a...

Descripción completa

Detalles Bibliográficos
Autores principales: Li, Wei, Zhao, Li-Chun, Wang, Zi, Zheng, Yi-Nan, Liang, Jian, Wang, Hui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3344203/
https://www.ncbi.nlm.nih.gov/pubmed/22605967
http://dx.doi.org/10.3390/ijms13044089
_version_ 1782231938945253376
author Li, Wei
Zhao, Li-Chun
Wang, Zi
Zheng, Yi-Nan
Liang, Jian
Wang, Hui
author_facet Li, Wei
Zhao, Li-Chun
Wang, Zi
Zheng, Yi-Nan
Liang, Jian
Wang, Hui
author_sort Li, Wei
collection PubMed
description In the present work, we reported the enzymatic preparation of deapio-platycodin D (dPD) and platycodin D (PD) optimized by response surface methodology (RSM) from Radix Platycodi. During investigation of the hydrolysis of crude platycosides by various glycoside hydrolases, snailase showed a strong ability to transform deapio-platycoside E (dPE) and platycoside E (PE) into dPD and PD with 100% conversion. RSM was used to optimize the effects of the reaction temperature (35–45 °C), enzyme load (5–20%), and reaction time (4–24 h) on the conversion process. Validation of the RSM model was verified by the good agreement between the experimental and the predicted values of dPD and PD conversion yield. The optimum preparation conditions were as follows: temperature, 43 °C; enzyme load, 15%; reaction time, 22 h. The biotransformation pathways were dPE→dPD3→dPD and PE→PD3→PD, respectively. The determined method may be highly applicable for the enzymatic preparation of dPD and PD for medicinal purposes and also for commercial use.
format Online
Article
Text
id pubmed-3344203
institution National Center for Biotechnology Information
language English
publishDate 2012
publisher Molecular Diversity Preservation International (MDPI)
record_format MEDLINE/PubMed
spelling pubmed-33442032012-05-17 Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi Li, Wei Zhao, Li-Chun Wang, Zi Zheng, Yi-Nan Liang, Jian Wang, Hui Int J Mol Sci Article In the present work, we reported the enzymatic preparation of deapio-platycodin D (dPD) and platycodin D (PD) optimized by response surface methodology (RSM) from Radix Platycodi. During investigation of the hydrolysis of crude platycosides by various glycoside hydrolases, snailase showed a strong ability to transform deapio-platycoside E (dPE) and platycoside E (PE) into dPD and PD with 100% conversion. RSM was used to optimize the effects of the reaction temperature (35–45 °C), enzyme load (5–20%), and reaction time (4–24 h) on the conversion process. Validation of the RSM model was verified by the good agreement between the experimental and the predicted values of dPD and PD conversion yield. The optimum preparation conditions were as follows: temperature, 43 °C; enzyme load, 15%; reaction time, 22 h. The biotransformation pathways were dPE→dPD3→dPD and PE→PD3→PD, respectively. The determined method may be highly applicable for the enzymatic preparation of dPD and PD for medicinal purposes and also for commercial use. Molecular Diversity Preservation International (MDPI) 2012-03-28 /pmc/articles/PMC3344203/ /pubmed/22605967 http://dx.doi.org/10.3390/ijms13044089 Text en © 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 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
Li, Wei
Zhao, Li-Chun
Wang, Zi
Zheng, Yi-Nan
Liang, Jian
Wang, Hui
Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi
title Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi
title_full Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi
title_fullStr Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi
title_full_unstemmed Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi
title_short Response Surface Methodology to Optimize Enzymatic Preparation of Deapio-Platycodin D and Platycodin D from Radix Platycodi
title_sort response surface methodology to optimize enzymatic preparation of deapio-platycodin d and platycodin d from radix platycodi
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3344203/
https://www.ncbi.nlm.nih.gov/pubmed/22605967
http://dx.doi.org/10.3390/ijms13044089
work_keys_str_mv AT liwei responsesurfacemethodologytooptimizeenzymaticpreparationofdeapioplatycodindandplatycodindfromradixplatycodi
AT zhaolichun responsesurfacemethodologytooptimizeenzymaticpreparationofdeapioplatycodindandplatycodindfromradixplatycodi
AT wangzi responsesurfacemethodologytooptimizeenzymaticpreparationofdeapioplatycodindandplatycodindfromradixplatycodi
AT zhengyinan responsesurfacemethodologytooptimizeenzymaticpreparationofdeapioplatycodindandplatycodindfromradixplatycodi
AT liangjian responsesurfacemethodologytooptimizeenzymaticpreparationofdeapioplatycodindandplatycodindfromradixplatycodi
AT wanghui responsesurfacemethodologytooptimizeenzymaticpreparationofdeapioplatycodindandplatycodindfromradixplatycodi