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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 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 (GenebankTM 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: 105 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 sed to characterize ulvan, e.g. through enzymatic/mass spectrometric fingerprinting analyses, and help unlock its full potential.

Titel: Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
Verfasser: Melcher, Rebecca L. J.
Neumann, Marten
Fuenzalida Werner, Juan Pablo GND
Gröhn, Franziska GND
Moerschbacher, Bruno M.
Organisation: FB 13: Biologie
Dokumenttyp: Artikel
Medientyp: Text
Erscheinungsdatum: 22.03.2017
Publikation in MIAMI: 26.10.2018
Datum der letzten Änderung: 26.10.2018
Quelle: Scientific Reports 7 (2017) Article number: 44115, 1-9
Fachgebiete: Biowissenschaften; Biologie
Lizenz: CC BY 4.0
Sprache: Englisch
Förderung: Finanziert durch den Open-Access-Publikationsfonds 2017 der Westfälischen Wilhelms-Universität Münster (WWU Münster).
Format: PDF-Dokument
URN: urn:nbn:de:hbz:6-17109674969
DOI: 10.1038/srep44115