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Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain

Biomass waste products from green algae have recently been given new life, as these polysaccharides have potential applications in industry, agriculture, and medicine. One such polysaccharide group called ulvans displays many different, potentially useful properties that arise from their structural...

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Autores principales: Melcher, Rebecca L. J., Neumann, Marten, Fuenzalida Werner, Juan Pablo, Gröhn, Franziska, Moerschbacher, Bruno M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5361163/
https://www.ncbi.nlm.nih.gov/pubmed/28327560
http://dx.doi.org/10.1038/srep44115
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author Melcher, Rebecca L. J.
Neumann, Marten
Fuenzalida Werner, Juan Pablo
Gröhn, Franziska
Moerschbacher, Bruno M.
author_facet Melcher, Rebecca L. J.
Neumann, Marten
Fuenzalida Werner, Juan Pablo
Gröhn, Franziska
Moerschbacher, Bruno M.
author_sort Melcher, Rebecca L. J.
collection PubMed
description Biomass waste products from green algae have recently been given new life, as these polysaccharides have potential applications in industry, agriculture, and medicine. One such polysaccharide group called ulvans displays many different, potentially useful properties that arise from their structural versatility. Hence, performing structural analyses on ulvan is crucial for future applications. However, chemical reaction–based analysis methods cannot fully characterize ulvan and tend to alter its structure. Thus, better methods require well-characterized ulvan-degrading enzymes. Therefore, we analysed a previously sequenced ulvan lyase (Genebank(TM) reference number JN104480) and characterized its domains. We suggest that the enzyme consists of a shorter than previously described catalytic domain, a newly identified substrate binding domain, and a C-terminal type 9 secretion system signal peptide. By separately expressing the two domains in E. coli, we confirmed that the binding domain is ulvan specific, having higher affinity for ulvan than most lectins for their ligands (affinity constant: 10(5) M(−1)). To our knowledge, this is the first description of an ulvan-binding domain. Overall, identifying this new binding domain is one step towards engineering ulvan enzymes that can be used to characterize ulvan, e.g. through enzymatic/mass spectrometric fingerprinting analyses, and help unlock its full potential.
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spelling pubmed-53611632017-03-24 Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain Melcher, Rebecca L. J. Neumann, Marten Fuenzalida Werner, Juan Pablo Gröhn, Franziska Moerschbacher, Bruno M. Sci Rep Article Biomass waste products from green algae have recently been given new life, as these polysaccharides have potential applications in industry, agriculture, and medicine. One such polysaccharide group called ulvans displays many different, potentially useful properties that arise from their structural versatility. Hence, performing structural analyses on ulvan is crucial for future applications. However, chemical reaction–based analysis methods cannot fully characterize ulvan and tend to alter its structure. Thus, better methods require well-characterized ulvan-degrading enzymes. Therefore, we analysed a previously sequenced ulvan lyase (Genebank(TM) reference number JN104480) and characterized its domains. We suggest that the enzyme consists of a shorter than previously described catalytic domain, a newly identified substrate binding domain, and a C-terminal type 9 secretion system signal peptide. By separately expressing the two domains in E. coli, we confirmed that the binding domain is ulvan specific, having higher affinity for ulvan than most lectins for their ligands (affinity constant: 10(5) M(−1)). To our knowledge, this is the first description of an ulvan-binding domain. Overall, identifying this new binding domain is one step towards engineering ulvan enzymes that can be used to characterize ulvan, e.g. through enzymatic/mass spectrometric fingerprinting analyses, and help unlock its full potential. Nature Publishing Group 2017-03-22 /pmc/articles/PMC5361163/ /pubmed/28327560 http://dx.doi.org/10.1038/srep44115 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Melcher, Rebecca L. J.
Neumann, Marten
Fuenzalida Werner, Juan Pablo
Gröhn, Franziska
Moerschbacher, Bruno M.
Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
title Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
title_full Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
title_fullStr Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
title_full_unstemmed Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
title_short Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
title_sort revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5361163/
https://www.ncbi.nlm.nih.gov/pubmed/28327560
http://dx.doi.org/10.1038/srep44115
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