Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota

A novel bacterial α 1–2-fucosyltransferase (α 2FT) from Thermosynechococcus sp. NK55a (Ts2FT) has been discovered and characterized. It shares 28–62% protein sequence homology to α 2FTs reported previously. The Ts2FT was cloned as an N-terminal His6-tagged recombinant protein (His6-Ts2FT) and expres...

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Autores principales:	Ruting Zhong, Luying Gao, Zhengxin Chen, Sinan Yuan, Xi Chen, Chao Zhao
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Carbohydrate Enzymatic synthesis Fucosyltransferase Fucosylated oligosaccharides Lacto-N-fucopentaose I Thermosynechococcus Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
Acceso en línea:	https://doaj.org/article/f4297c6ef7ae47d6a4e5eee7e47bbace
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spelling	oai:doaj.org-article:f4297c6ef7ae47d6a4e5eee7e47bbace2021-11-14T04:35:24ZChemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota2590-157510.1016/j.fochx.2021.100152https://doaj.org/article/f4297c6ef7ae47d6a4e5eee7e47bbace2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2590157521000407https://doaj.org/toc/2590-1575A novel bacterial α 1–2-fucosyltransferase (α 2FT) from Thermosynechococcus sp. NK55a (Ts2FT) has been discovered and characterized. It shares 28–62% protein sequence homology to α 2FTs reported previously. The Ts2FT was cloned as an N-terminal His6-tagged recombinant protein (His6-Ts2FT) and expressed in E. coli BL21 (DE3). It was expressed at a level of 6.2 mg/L culture after induction with 0.05 mM of isopropylβ-d-1-thiogalactoside (IPTG) at 16 °C for 20 h. It showed the optimal activity at a reaction temperature of 40 °C and pH of 7.0. The presence of a Mg2+ improved its catalytic efficiency. Ts2FT displayed a strict acceptor specificity and could recognize only β1–3-galatoside acceptors. It was used efficiently for one-pot multienzyme synthesis of fucosylated oligosaccharides. One of the products, lacto-N-fucopentaose I was shown to promote the growth of intestinal probiotics including those belonging to Acidobacteria, Actinobacteria, Proteobacteria, Planctomycetes, and Chloroflexi.Ruting ZhongLuying GaoZhengxin ChenSinan YuanXi ChenChao ZhaoElsevierarticleCarbohydrateEnzymatic synthesisFucosyltransferaseFucosylated oligosaccharidesLacto-N-fucopentaose IThermosynechococcusNutrition. Foods and food supplyTX341-641Food processing and manufactureTP368-456ENFood Chemistry: X, Vol 12, Iss , Pp 100152- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Carbohydrate Enzymatic synthesis Fucosyltransferase Fucosylated oligosaccharides Lacto-N-fucopentaose I Thermosynechococcus Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
spellingShingle	Carbohydrate Enzymatic synthesis Fucosyltransferase Fucosylated oligosaccharides Lacto-N-fucopentaose I Thermosynechococcus Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456 Ruting Zhong Luying Gao Zhengxin Chen Sinan Yuan Xi Chen Chao Zhao Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota
description	A novel bacterial α 1–2-fucosyltransferase (α 2FT) from Thermosynechococcus sp. NK55a (Ts2FT) has been discovered and characterized. It shares 28–62% protein sequence homology to α 2FTs reported previously. The Ts2FT was cloned as an N-terminal His6-tagged recombinant protein (His6-Ts2FT) and expressed in E. coli BL21 (DE3). It was expressed at a level of 6.2 mg/L culture after induction with 0.05 mM of isopropylβ-d-1-thiogalactoside (IPTG) at 16 °C for 20 h. It showed the optimal activity at a reaction temperature of 40 °C and pH of 7.0. The presence of a Mg2+ improved its catalytic efficiency. Ts2FT displayed a strict acceptor specificity and could recognize only β1–3-galatoside acceptors. It was used efficiently for one-pot multienzyme synthesis of fucosylated oligosaccharides. One of the products, lacto-N-fucopentaose I was shown to promote the growth of intestinal probiotics including those belonging to Acidobacteria, Actinobacteria, Proteobacteria, Planctomycetes, and Chloroflexi.
format	article
author	Ruting Zhong Luying Gao Zhengxin Chen Sinan Yuan Xi Chen Chao Zhao
author_facet	Ruting Zhong Luying Gao Zhengxin Chen Sinan Yuan Xi Chen Chao Zhao
author_sort	Ruting Zhong
title	Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota
title_short	Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota
title_full	Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota
title_fullStr	Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota
title_full_unstemmed	Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota
title_sort	chemoenzymatic synthesis of fucosylated oligosaccharides using thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/f4297c6ef7ae47d6a4e5eee7e47bbace
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Chemoenzymatic synthesis of fucosylated oligosaccharides using Thermosynechococcus α1–2-fucosyltransferase and their application in the regulation of intestinal microbiota

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