Production, purification, and preliminary biochemical characterization of a family 127 glycoside hydrolase from the marine bacterium Zobellia galactanivorans - Preliminary study of putative bacterial arabinogalactan protein utilization operon

Bioinformatic analysis reveal that the marine bacterium Zobellia galactanivorans possesses an operon like structure with 18 genes comprising four enzymes belonging to two novel glycoside hydrolase families; three enzymes (GH127-1, GH127-2, & GH127-3) of GH127 family and one enzyme of GH129. A synergistic effect on degrading a common substrate is therefore hypothesized. Representative enzymes from the GH127 and GH129 families have been previously characterized as β-L-arabinofuranose and α-N-acetylgalactosaminidase respectively. Based on the amino acid sequence similarity within a GH family, a similar enzymatic activity is assumed for enzymes from Z. galactanivorans. Arabinogalactan-like protein, a glycoprotein built from amino acid backbone with galactan and arabinose component was recently found in brown algae, is a potential substrate. GH127-1 and GH127-2 enzymes were produced recombinantly and purified. Crystals of GH127-1 could be grown and were diffracted X-ray at ~3Å. Enzymatic digestion of substrate analogs with different combinations of the GH127-1, Gh127-2, and G129 enzymes showed no positive activity. Though, interestingly GH129 demonstrated possible transglycosylation activity on purified fraction of potato galactan.

ISCED Categories

The highlighted icons, represent the fields of education (in compliance with ISCED Classification) engaged during this course/programme.