Substrate specificity of the recombinant alginate lyase from the marine bacteria Pseudomonas alginovora.
作者： Lena C.E. Lundqvist , Murielle Jam , Tristan Barbeyron , Mirjam Czjzek , Corine Sandström
DOI: 10.1016/J.CARRES.2012.02.014
关键词:
摘要: The gene coding for an alginate lyase from the marine bacteria Pseudomonas alginovora X017 was cloned and heterologously expressed in Escherichia coli strains. protein produced inclusion bodies active form obtained by applying a refolding protocol based upon dilution. biochemical characterization performed on active, refolded of lyase. substrate specificity monitored NMR. degradation products were size-fractioned size exclusion chromatography. fractions subsequently analyzed ESI-MS to determine molecular weight compounds. structures different oligosaccharides then elucidated enzyme shown be only acting M-M diads. No enzymatic hydrolysis occurred between M-MG, G-MM or G-MG blocks proving that sequence accounting generated oligomers is M-MM. unsaturated ΔM, ΔMM, ΔMMM, ΔMMMM indicating minimum structure recognized M6 oligosaccharide.
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