@misc{9230717,
  abstract     = {{This study aimed to screen and characterize unknown glucuronoyl esterases (GEs) belonging to bacterial carbohydrate esterase family 15 (CE15), which were CE15_6nl, CE15_13nl, and CE15_15nsp. First, purified proteins were obtained by heterologous expression in E. coli induced by IPTG. Next, nanoDSF assays were performed to determine the thermostability of CE15 enzymes under different pH conditions, CE15_6nl and CE15_15nsp were most stable under pH 7 and pH 6.5, respectively, whereas CE15_13nl was more stable under alkaline conditions. Moreover, kinetics parameters were determined by coupled continuous assays on three model substrates. CE15_15nsp exhibited the highest catalytic efficiency and substrate affinity among the three enzymes. All candidates showed a preference for long substrates. To explore the action of single CE15 enzyme and CE15-GH30 synergy in the hydrolysis of natural biomass such as corn bran, HPAEC-PAD analysis was conducted. The results suggested that CE15 enzymes promoted the release of xylose and xylo-oligosaccharides, however, no synergistic effect between CE15 and GH30 could be detected. In total, CE15 enzymes show promising potential in lignocellulosic biomass processing, but further analytical experiments are required.}},
  author       = {{Wang, Junyang}},
  language     = {{eng}},
  note         = {{Student Paper}},
  title        = {{Screening and Characterization of Glucuronoyl Esterase Candidates from the CE15 Family}},
  year         = {{2026}},
}