Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.

Cellulosic biomass is an abundant and promising energy source. To make cellulosic biofuels competitive against conventional fuels, conversion of rigid plant materials into sugars must become efficient and cost-effective. During cellulose degradation, cellulolytic enzymes generate cellobiose (β-(1→4)...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Aki Yoneda, Hsion-Wen David Kuo, Mayumi Ishihara, Parastoo Azadi, Su-May Yu, Tuan-hua David Ho
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a7d306782dcb411e98c8a56d0819af62
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:a7d306782dcb411e98c8a56d0819af62
record_format	dspace
spelling	oai:doaj.org-article:a7d306782dcb411e98c8a56d0819af622021-11-25T06:02:17ZGlycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.1932-620310.1371/journal.pone.0106306https://doaj.org/article/a7d306782dcb411e98c8a56d0819af622014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25180973/?tool=EBIhttps://doaj.org/toc/1932-6203Cellulosic biomass is an abundant and promising energy source. To make cellulosic biofuels competitive against conventional fuels, conversion of rigid plant materials into sugars must become efficient and cost-effective. During cellulose degradation, cellulolytic enzymes generate cellobiose (β-(1→4)-glucose dimer) molecules, which in turn inhibit such enzymes by negative feedback. β-Glucosidases (BGLs) cleave cellobiose into glucose monomers, assisting overall cellulolytic activities. Therefore, BGLs are essential for efficient conversion of cellulosic biomass into biofuels, and it is important to characterize newly isolated BGLs for useful traits. Here, we report our discovery that the indigenous Taiwanese fungus Chaetomella raphigera strain D2 produces two molecular weight variants of a single BGL, D2-BGL (shortened to "D2"), which differ in O-glycosylation. The more extensively O-glycosylated form of native D2 (nD2L) has increased activity toward the natural substrate, cellobiose, compared to the less O-glycosylated form (nD2S). nD2L is more stable at 60°C, in acidic pH, and in the presence of the ionic detergent sodium dodecyl sulfate than nD2S. Furthermore, unlike nD2S, nD2L does not display substrate inhibition by an artificial substrate p-nitrophenyl glucopyranoside (pNPG), and the glucose feedback inhibition kinetics of nD2L is competitive (while it is non-competitive for nD2S), suggesting that these two glycovariants of D2 bind substrates differently. Interestingly, D2 produced in a heterologous system, Pichia pastoris, closely mimics properties of nD2S. Our studies suggest that O-glycosylation of D2 is important in determining its catalytic and biochemical properties.Aki YonedaHsion-Wen David KuoMayumi IshiharaParastoo AzadiSu-May YuTuan-hua David HoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 9, p e106306 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Aki Yoneda Hsion-Wen David Kuo Mayumi Ishihara Parastoo Azadi Su-May Yu Tuan-hua David Ho Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.
description	Cellulosic biomass is an abundant and promising energy source. To make cellulosic biofuels competitive against conventional fuels, conversion of rigid plant materials into sugars must become efficient and cost-effective. During cellulose degradation, cellulolytic enzymes generate cellobiose (β-(1→4)-glucose dimer) molecules, which in turn inhibit such enzymes by negative feedback. β-Glucosidases (BGLs) cleave cellobiose into glucose monomers, assisting overall cellulolytic activities. Therefore, BGLs are essential for efficient conversion of cellulosic biomass into biofuels, and it is important to characterize newly isolated BGLs for useful traits. Here, we report our discovery that the indigenous Taiwanese fungus Chaetomella raphigera strain D2 produces two molecular weight variants of a single BGL, D2-BGL (shortened to "D2"), which differ in O-glycosylation. The more extensively O-glycosylated form of native D2 (nD2L) has increased activity toward the natural substrate, cellobiose, compared to the less O-glycosylated form (nD2S). nD2L is more stable at 60°C, in acidic pH, and in the presence of the ionic detergent sodium dodecyl sulfate than nD2S. Furthermore, unlike nD2S, nD2L does not display substrate inhibition by an artificial substrate p-nitrophenyl glucopyranoside (pNPG), and the glucose feedback inhibition kinetics of nD2L is competitive (while it is non-competitive for nD2S), suggesting that these two glycovariants of D2 bind substrates differently. Interestingly, D2 produced in a heterologous system, Pichia pastoris, closely mimics properties of nD2S. Our studies suggest that O-glycosylation of D2 is important in determining its catalytic and biochemical properties.
format	article
author	Aki Yoneda Hsion-Wen David Kuo Mayumi Ishihara Parastoo Azadi Su-May Yu Tuan-hua David Ho
author_facet	Aki Yoneda Hsion-Wen David Kuo Mayumi Ishihara Parastoo Azadi Su-May Yu Tuan-hua David Ho
author_sort	Aki Yoneda
title	Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.
title_short	Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.
title_full	Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.
title_fullStr	Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.
title_full_unstemmed	Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.
title_sort	glycosylation variants of a β-glucosidase secreted by a taiwanese fungus, chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/a7d306782dcb411e98c8a56d0819af62
work_keys_str_mv	AT akiyoneda glycosylationvariantsofabglucosidasesecretedbyataiwanesefunguschaetomellaraphigeraexhibitvariantspecificcatalyticandbiochemicalproperties AT hsionwendavidkuo glycosylationvariantsofabglucosidasesecretedbyataiwanesefunguschaetomellaraphigeraexhibitvariantspecificcatalyticandbiochemicalproperties AT mayumiishihara glycosylationvariantsofabglucosidasesecretedbyataiwanesefunguschaetomellaraphigeraexhibitvariantspecificcatalyticandbiochemicalproperties AT parastooazadi glycosylationvariantsofabglucosidasesecretedbyataiwanesefunguschaetomellaraphigeraexhibitvariantspecificcatalyticandbiochemicalproperties AT sumayyu glycosylationvariantsofabglucosidasesecretedbyataiwanesefunguschaetomellaraphigeraexhibitvariantspecificcatalyticandbiochemicalproperties AT tuanhuadavidho glycosylationvariantsofabglucosidasesecretedbyataiwanesefunguschaetomellaraphigeraexhibitvariantspecificcatalyticandbiochemicalproperties
_version_	1718414299833040896

Glycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical properties.

Ejemplares similares