Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides

Abstract Humans have exploited natural resources for a variety of applications. Chitin and its derivative chitin oligosaccharides (CHOS) have potential biomedical and agricultural applications. Availability of CHOS with the desired length has been a major limitation in the optimum use of such natura...

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Autores principales:	Mohan Krishna Mallakuntla, Papa Rao Vaikuntapu, Bhoopal Bhuvanachandra, Subha Narayan Das, Appa Rao Podile
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d978bfdb29324565a6edf7e33c313060
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spelling	oai:doaj.org-article:d978bfdb29324565a6edf7e33c3130602021-12-02T16:06:24ZTransglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides10.1038/s41598-017-05140-32045-2322https://doaj.org/article/d978bfdb29324565a6edf7e33c3130602017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05140-3https://doaj.org/toc/2045-2322Abstract Humans have exploited natural resources for a variety of applications. Chitin and its derivative chitin oligosaccharides (CHOS) have potential biomedical and agricultural applications. Availability of CHOS with the desired length has been a major limitation in the optimum use of such natural resources. Here, we report a single domain hyper-transglycosylating chitinase, which generates longer CHOS, from Enterobacter cloacae subsp. cloacae 13047 (EcChi1). EcChi1 was optimally active at pH 5.0 and 40 °C with a Km of 15.2 mg ml−1, and k cat/Km of 0.011× 102 mg−1 ml min−1 on colloidal chitin. The profile of the hydrolytic products, major product being chitobiose, released from CHOS indicated that EcChi1 was an endo-acting enzyme. Transglycosylation (TG) by EcChi1 on trimeric to hexameric CHOS resulted in the formation of longer CHOS for a prolonged duration. EcChi1 showed both chitobiase and TG activities, in addition to hydrolytic activity. The TG by EcChi1 was dependent, to some extent, on the length of the CHOS substrate and concentration of the enzyme. Homology modeling and docking with CHOS suggested that EcChi1 has a deep substrate-binding groove lined with aromatic amino acids, which is a characteristic feature of a processive enzyme.Mohan Krishna MallakuntlaPapa Rao VaikuntapuBhoopal BhuvanachandraSubha Narayan DasAppa Rao PodileNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mohan Krishna Mallakuntla Papa Rao Vaikuntapu Bhoopal Bhuvanachandra Subha Narayan Das Appa Rao Podile Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides
description	Abstract Humans have exploited natural resources for a variety of applications. Chitin and its derivative chitin oligosaccharides (CHOS) have potential biomedical and agricultural applications. Availability of CHOS with the desired length has been a major limitation in the optimum use of such natural resources. Here, we report a single domain hyper-transglycosylating chitinase, which generates longer CHOS, from Enterobacter cloacae subsp. cloacae 13047 (EcChi1). EcChi1 was optimally active at pH 5.0 and 40 °C with a Km of 15.2 mg ml−1, and k cat/Km of 0.011× 102 mg−1 ml min−1 on colloidal chitin. The profile of the hydrolytic products, major product being chitobiose, released from CHOS indicated that EcChi1 was an endo-acting enzyme. Transglycosylation (TG) by EcChi1 on trimeric to hexameric CHOS resulted in the formation of longer CHOS for a prolonged duration. EcChi1 showed both chitobiase and TG activities, in addition to hydrolytic activity. The TG by EcChi1 was dependent, to some extent, on the length of the CHOS substrate and concentration of the enzyme. Homology modeling and docking with CHOS suggested that EcChi1 has a deep substrate-binding groove lined with aromatic amino acids, which is a characteristic feature of a processive enzyme.
format	article
author	Mohan Krishna Mallakuntla Papa Rao Vaikuntapu Bhoopal Bhuvanachandra Subha Narayan Das Appa Rao Podile
author_facet	Mohan Krishna Mallakuntla Papa Rao Vaikuntapu Bhoopal Bhuvanachandra Subha Narayan Das Appa Rao Podile
author_sort	Mohan Krishna Mallakuntla
title	Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides
title_short	Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides
title_full	Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides
title_fullStr	Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides
title_full_unstemmed	Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides
title_sort	transglycosylation by a chitinase from enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d978bfdb29324565a6edf7e33c313060
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Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides

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