@misc{9230576,
  abstract     = {{Carbohydrate esterase family 1 (CE1) enzymes are a diverse group of enzymes involved in plant biomass degradation through removal of acetyl and feruloyl substitutions from polysaccharides. In this study, several putative CE1 enzymes were characterized to find out their substrate preference, catalytic properties and possible role during biomass hydrolysis. Functional screening using pNP-acetate and pNP-ferulate showed clear differences between the analyzed enzymes. AXE2 and FAE9 were active toward both substrates, whereas ACE3 showed lower activity and appeared to hydrolyze acetyl ester substrates. Kinetic analysis showed differences between AXE2 and FAE9, where AXE2 showed stronger affinity toward ferulate (Km = 0.821±0.127 mM), while FAE9 displayed higher catalytic turnover and catalytic efficiency toward pNP-acetate, with a kcat of 37.414 ± 3.217 min-1 and catalytic efficiency of 43.692 ± 3.495 mM-1min-1. The hydrolysis experiments performed with the GH11 xylanase Pentopan Mono BG resulted in noticeable changes in oligosaccharide profiles across several biomass substrates, particularly for arabinoxylan and xylan-rich substrates, suggesting possible synergy between the CE1 enzymes and the GH11 xylanase during biomass degradation. Hence, the findings agree with the proposed accessory role of CE1 enzymes in biomass hydrolysis and provide insight into their possible use in enzymatic biomass conversion systems.}},
  author       = {{Nayak, Rithika Vivekananda}},
  language     = {{eng}},
  note         = {{Student Paper}},
  title        = {{Biochemical Characterization on CE1 Carbohydrate Esterases with Potential Dual Esterase Activity}},
  year         = {{2026}},
}