Process Biochemistry
Process Biochemistry
4 years ago

Overexpression and characterization of a novel α-neoagarobiose hydrolase and its application in the production of D-galactonate from Gelidium amansii

Overexpression and characterization of a novel α-neoagarobiose hydrolase and its application in the production of D-galactonate from Gelidium amansii
An α-neoagarobiose hydrolase (α-NABH) from Cellulophaga sp. W5C, designated as AhgI, was identified, purified, and characterized. Its 1227 base pairs of coded sequence translate into a 408-amino acid protein that belongs to the GH117 family. Multiple sequence alignment of AhgI with other known α-NABHs showed 83% homology with AhgA from Zobellia galactanivorans. AhgI had an apparent molecular weight of 45kDa and was highly active at pH 7.0 and 20°C. The K m and V max values for neoagarobiose (NA2) were 1.03mM and 10.22U/mg, respectively. Apart from NA2, the enzyme showed activity against other neoagaro-oligosaccharides (NAOSs) such as neoagarotetraose (NA4) and neoagarohexaose (NA6). AhgI was then employed in a prototype process to produce D-galactonate from Gelidium amansii. Agar from G. amansii was hydrothermally extracted and then enzymatically hydrolyzed by sequential addition of β-agarases and AhgI. The final hydrolysate containing D-galactose was then utilized for the microbial production of D-galactonate. This is believed to be the first report on the identification and characterization of an α-NABH derived from Cellulophaga species and its subsequent application in the synthesis of a value-added chemical directly from marine macroalgae.

Publisher URL: www.sciencedirect.com/science

DOI: S135951131730939X

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