Understanding xylose isomerase from Burkholderia cenocepacia: insights into structure and functionality for ethanol production.

ABSTRACT: The inability of the yeast Saccharomyces cerevisiae to produce ethanol from xylose has hampered the biofuel production from lignocellulosic biomass. However, prior studies reveal that functional expression of xylose isomerase (XI) from Burkholderia cenocepacia (XylA_Bc) in S. cerevisiae has remarkably improved xylose consumption and ethanol productivity. Yet, little is known about kinetic and structural properties of this enzyme. Hereby, a purified recombinant XylA was assayed in vitro, showing optimal enzyme activity at 37 °C and pH 7.2. The K_m of XylA for D-xylose was at least threefold lower than the K_m results for any XI published to date (e.g. XylA from Piromyces sp.). In addition, oligomerization behavior as a tetramer was observed for XylA in solution

SUBMITTER: Vieira IPV 

PROVIDER: S-EPMC6534634 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature