535960-67-9

Upstream product

• 59997-94-3 p-nitrophenyl 2,3-di-O-acetyl-α-L-arabinofuranoside 
• 50906-12-2 4-acetoxy-3-methoxycinnamoyl chloride 
• 535960-64-6 4-nitrophenyl 2,3,6-tri-O-acetyl-5-deoxy-α-L-arabino-hexofuranoside 

Downstream Products

• 22796-65-2 p-nitrophenyl α-L-arabinofuranoside 

Relevant academic research and scientific papers

Preparation of regioselectively feruloylated p-nitrophenyl α-l-arabinofuranosides and β-d-xylopyranosides-convenient substrates for study of feruloyl esterase specificity

p-Nitrophenyl α-l-arabinofuranoside and β-d-xylopyranoside mono-O-ferulates were prepared by 4-O-acetylferuloylation of corresponding enzymatically prepared di-O-acetates followed by deacetylation. An alternative mild acylation catalysed by zinc oxide was tested on xylopyranoside derivatives. The chemoselective methanolysis of the acetyl groups using neutral catalyst dibutyltin oxide at reflux was used as deacetylation method. Under these conditions a significant feruloyl migration was observed mainly on p-nitrophenyl 3-O-feruloyl-β-d-xylopyranoside resulting in low yields of the positional isomers. Investigation of substrate and positional specificity of different types of feruloyl esterases on the presented compounds in enzyme-coupled assays was reported previously.

Two efficient ways to 2-O- and 5-O-feruloylated 4-nitrophenyl α-L-arabinofuranosides as substrates for differentiation of feruloyl esterases

4-Nitrophenyl 2-O-(E)-feruloyl-α-L-arabinofuranoside 1 and 4-nitrophenyl 5-O-(E)-feruloyl-α-L-arabinofuranoside 2 have been synthesized by two different routes. Monoferuloylation was accomplished by a chemoenzymatic sequence employing a regioselective transesterification catalyzed by lipases. The feruloyl group was introduced to enzymatically prepared 2,3- and 3,5-diacetates of 4-nitrophenyl α-L-arabinofuranoside by reaction with 4-O-acetylferuloyl chloride. Removal of the protecting acetyl groups yielded 1 and 2. An alternative chemical synthesis suitable for preparation of larger quantities of 1 and 2 also is presented. The new substrates represent convenient tools to differentiate feruloyl esterases on the basis of their substrate specificity.