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![[Figure 5]](jc5061fig5mag.jpg)
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Figure 5
Product formation from Mef1 hydrolysis of fucoidan from F. evanescens as monitored by NMR spectroscopy. (a) In situ 1H–13C NMR spectroscopy of the degradation of fucoidan after 20 min (black), 120 min (gray), 400 min (green) and 800 min (blue) at 303 K and pH 8.0. The emergence of reducing-end signals and other transitions from substrate to product signals are due to enzyme activity. Spectra were manually offset in the 1H dimension by −0.02 p.p.m. between the time points for clarity, showing that glycosidic bonds at the anomeric C atom of 3)-α-Fucp-2-SO3−-(1,4) residues are broken, while structural motifs containing 3)-α-Fucp-2,4-di-SO3−-(1,4)-α-Fuc-2-SO3−-(1,3) repeating units remain intact. (b) 1H NMR spectra of F. evanescens fucoidan (fucoidan) and the low-molecular-weight product fraction upon degradation with Mef1 (fucoidan + Mef1). (c) Molecular structure of the tetrasaccharide constituting the principal low-molecular-weight hydrolysis product (LMP) upon degradation of F. evanescens fucoidan by Mef1. |
![[Figure 5]](jc5061fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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