Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.

Isoflavone occurs abundantly in leguminous seeds in the form of glycoside and aglycone. However, isoflavone glycoside has anti-nutritional effect and only the free type is beneficial to human health. In the present study we identified a β-glucosidase from thermophilic Neosartorya fischeri P1, termed...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Xinzhuo Yang, Rui Ma, Pengjun Shi, Huoqing Huang, Yingguo Bai, Yaru Wang, Peilong Yang, Yunliu Fan, Bin Yao
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/85b99a7ebd0e4bdfa8ebcf7c9b1166ba
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:85b99a7ebd0e4bdfa8ebcf7c9b1166ba
record_format	dspace
spelling	oai:doaj.org-article:85b99a7ebd0e4bdfa8ebcf7c9b1166ba2021-11-25T06:01:52ZMolecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.1932-620310.1371/journal.pone.0106785https://doaj.org/article/85b99a7ebd0e4bdfa8ebcf7c9b1166ba2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25188254/?tool=EBIhttps://doaj.org/toc/1932-6203Isoflavone occurs abundantly in leguminous seeds in the form of glycoside and aglycone. However, isoflavone glycoside has anti-nutritional effect and only the free type is beneficial to human health. In the present study we identified a β-glucosidase from thermophilic Neosartorya fischeri P1, termed NfBGL1, capable of efficiently converting isoflavone glycosides into free isoflavones. The gene, belonging to glycoside hydrolase family 3, was successfully overexpressed in Pichia pastoris at high cell density in a 3.7-l fermentor. Purified recombinant NfBGL1 had higher specific activity (2189 ± 1.7 U/mg) and temperature optimum (80 °C) than other fungal counterparts when using p-nitrophenyl β-D-glucopyranoside as the substrate. It retained stable at temperatures up to 70 °C and over a broad pH range of 3.0-10.0. NfBGL1 had broad substrate specificity including glucosidase, cellobiase, xylanase and glucanase activities, and displayed preference for hydrolysis of β-1,2 glycosidic bond rather than β-1,3, β-1,4, β-1,6 bonds. The enzyme showed high bioconversion ability for major soybean isoflavone glycosides (daidin, gensitin and glycitin) into free forms. These properties make NfBGL1 potential for the wide use in the food, feed, pharmacy and biofuel industries.Xinzhuo YangRui MaPengjun ShiHuoqing HuangYingguo BaiYaru WangPeilong YangYunliu FanBin YaoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 9, p e106785 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xinzhuo Yang Rui Ma Pengjun Shi Huoqing Huang Yingguo Bai Yaru Wang Peilong Yang Yunliu Fan Bin Yao Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.
description	Isoflavone occurs abundantly in leguminous seeds in the form of glycoside and aglycone. However, isoflavone glycoside has anti-nutritional effect and only the free type is beneficial to human health. In the present study we identified a β-glucosidase from thermophilic Neosartorya fischeri P1, termed NfBGL1, capable of efficiently converting isoflavone glycosides into free isoflavones. The gene, belonging to glycoside hydrolase family 3, was successfully overexpressed in Pichia pastoris at high cell density in a 3.7-l fermentor. Purified recombinant NfBGL1 had higher specific activity (2189 ± 1.7 U/mg) and temperature optimum (80 °C) than other fungal counterparts when using p-nitrophenyl β-D-glucopyranoside as the substrate. It retained stable at temperatures up to 70 °C and over a broad pH range of 3.0-10.0. NfBGL1 had broad substrate specificity including glucosidase, cellobiase, xylanase and glucanase activities, and displayed preference for hydrolysis of β-1,2 glycosidic bond rather than β-1,3, β-1,4, β-1,6 bonds. The enzyme showed high bioconversion ability for major soybean isoflavone glycosides (daidin, gensitin and glycitin) into free forms. These properties make NfBGL1 potential for the wide use in the food, feed, pharmacy and biofuel industries.
format	article
author	Xinzhuo Yang Rui Ma Pengjun Shi Huoqing Huang Yingguo Bai Yaru Wang Peilong Yang Yunliu Fan Bin Yao
author_facet	Xinzhuo Yang Rui Ma Pengjun Shi Huoqing Huang Yingguo Bai Yaru Wang Peilong Yang Yunliu Fan Bin Yao
author_sort	Xinzhuo Yang
title	Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.
title_short	Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.
title_full	Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.
title_fullStr	Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.
title_full_unstemmed	Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.
title_sort	molecular characterization of a highly-active thermophilic β-glucosidase from neosartorya fischeri p1 and its application in the hydrolysis of soybean isoflavone glycosides.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/85b99a7ebd0e4bdfa8ebcf7c9b1166ba
work_keys_str_mv	AT xinzhuoyang molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT ruima molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT pengjunshi molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT huoqinghuang molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT yingguobai molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT yaruwang molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT peilongyang molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT yunliufan molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides AT binyao molecularcharacterizationofahighlyactivethermophilicbglucosidasefromneosartoryafischerip1anditsapplicationinthehydrolysisofsoybeanisoflavoneglycosides
_version_	1718414292808630272

Molecular characterization of a highly-active thermophilic β-glucosidase from Neosartorya fischeri P1 and its application in the hydrolysis of soybean isoflavone glycosides.

Ejemplares similares