Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass

Abstract Cellulolytic enzymes capable of hydrolyzing plant biomass are secreted by microbial cells specifically in response to the carbon substrate present in the environment. These enzymes consist of a catalytic domain, generally appended to one or more non-catalytic Carbohydrate Binding Module (CB...

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Autores principales:	Nandita Pasari, Nidhi Adlakha, Mayank Gupta, Zeenat Bashir, Girish H. Rajacharya, Garima Verma, Manoj Munde, Rakesh Bhatnagar, Syed Shams Yazdani
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/04a61df7867e4e64816782d6cea0225a
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spelling	oai:doaj.org-article:04a61df7867e4e64816782d6cea0225a2021-12-02T15:05:24ZImpact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass10.1038/s41598-017-03927-y2045-2322https://doaj.org/article/04a61df7867e4e64816782d6cea0225a2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03927-yhttps://doaj.org/toc/2045-2322Abstract Cellulolytic enzymes capable of hydrolyzing plant biomass are secreted by microbial cells specifically in response to the carbon substrate present in the environment. These enzymes consist of a catalytic domain, generally appended to one or more non-catalytic Carbohydrate Binding Module (CBM), which enhances their activity towards recalcitrant biomass. In the present study, the genome of a cellulolytic microbe Paenibacillus polymyxa A18 was annotated for the presence of CBMs and analyzed their expression in response to the plant biomass and model polysaccharides Avicel, CMC and xylan using quantitative PCR. A gene that encodes X2-CBM3 was found to be maximally induced in response to the biomass and crystalline substrate Avicel. Association of X2-CBM3 with xyloglucanase and endoglucanase led to up to 4.6-fold increase in activity towards insoluble substrates. In the substrate binding study, module X2 showed a higher affinity towards biomass and phosphoric acid swollen cellulose, whereas CBM3 showed a higher affinity towards Avicel. Further structural modeling of X2 also indicated its potential role in substrate binding. Our findings highlighted the role of module X2 along with CBM3 in assisting the enzyme catalysis of agricultural residue and paved the way to engineer glycoside hydrolases for superior activity.Nandita PasariNidhi AdlakhaMayank GuptaZeenat BashirGirish H. RajacharyaGarima VermaManoj MundeRakesh BhatnagarSyed Shams YazdaniNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nandita Pasari Nidhi Adlakha Mayank Gupta Zeenat Bashir Girish H. Rajacharya Garima Verma Manoj Munde Rakesh Bhatnagar Syed Shams Yazdani Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass
description	Abstract Cellulolytic enzymes capable of hydrolyzing plant biomass are secreted by microbial cells specifically in response to the carbon substrate present in the environment. These enzymes consist of a catalytic domain, generally appended to one or more non-catalytic Carbohydrate Binding Module (CBM), which enhances their activity towards recalcitrant biomass. In the present study, the genome of a cellulolytic microbe Paenibacillus polymyxa A18 was annotated for the presence of CBMs and analyzed their expression in response to the plant biomass and model polysaccharides Avicel, CMC and xylan using quantitative PCR. A gene that encodes X2-CBM3 was found to be maximally induced in response to the biomass and crystalline substrate Avicel. Association of X2-CBM3 with xyloglucanase and endoglucanase led to up to 4.6-fold increase in activity towards insoluble substrates. In the substrate binding study, module X2 showed a higher affinity towards biomass and phosphoric acid swollen cellulose, whereas CBM3 showed a higher affinity towards Avicel. Further structural modeling of X2 also indicated its potential role in substrate binding. Our findings highlighted the role of module X2 along with CBM3 in assisting the enzyme catalysis of agricultural residue and paved the way to engineer glycoside hydrolases for superior activity.
format	article
author	Nandita Pasari Nidhi Adlakha Mayank Gupta Zeenat Bashir Girish H. Rajacharya Garima Verma Manoj Munde Rakesh Bhatnagar Syed Shams Yazdani
author_facet	Nandita Pasari Nidhi Adlakha Mayank Gupta Zeenat Bashir Girish H. Rajacharya Garima Verma Manoj Munde Rakesh Bhatnagar Syed Shams Yazdani
author_sort	Nandita Pasari
title	Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass
title_short	Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass
title_full	Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass
title_fullStr	Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass
title_full_unstemmed	Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass
title_sort	impact of module-x2 and carbohydrate binding module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/04a61df7867e4e64816782d6cea0225a
work_keys_str_mv	AT nanditapasari impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT nidhiadlakha impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT mayankgupta impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT zeenatbashir impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT girishhrajacharya impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT garimaverma impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT manojmunde impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT rakeshbhatnagar impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass AT syedshamsyazdani impactofmodulex2andcarbohydratebindingmodule3onthecatalyticactivityofassociatedglycosidehydrolasestowardsplantbiomass
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Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass

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