TY  - JOUR
AB  - 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.
AU  - Melcher, Rebecca
AU  - Neumann, Marten
AU  - Fuenzalida Werner, Juan Pablo
AU  - Fuenzalida-Werner, Juan Pablo
AU  - Werner, Juan Pablo Fuenzalida
AU  - Fuenzalida, J. P.
AU  - Fuenzalida, Juan Pablo
AU  - Gröhn, Franziska
AU  - Moerschbacher, Bruno
DA  - 2017-03-22
DO  - 10.1038/srep44115
LA  - eng
N1  - Scientific Reports 7 (2017) Article number: 44115, 1-9
N1  - Finanziert durch den Open-Access-Publikationsfonds 2017 der Westfälischen Wilhelms-Universität Münster (WWU Münster).
PY  - 2017-03-22
TI  - Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain
UR  - https://nbn-resolving.org/urn:nbn:de:hbz:6-17109674969
Y2  - 2024-11-22T04:20:23
ER  -