1365626-51-2

Upstream product

• 141-78-6 ethyl acetate 
• 501669-17-6 (±)-1,3,6-tri-O-benzyl-myo-inositol 
• 108-24-7 acetic anhydride 
• 108-22-5 Isopropenyl acetate 
• 108-05-4 vinyl acetate 
• 98906-25-3 (±)-1,2-O-isopropylidene-3,6-di-O-benzyl-myo-inositol 
• 100-39-0 benzyl bromide 
• 115184-71-9 (+/-)-1,3,4-tri-O-benzyl-myo-inositol 
• 35949-67-8 (±)-1,4-di-O-benzyl-myo-inositol 

Relevant academic research and scientific papers

Kinetic resolution of 1,3,6-tri-O-benzyl-myo-inositol by Novozym 435: Optimization and enzyme reuse

myo-Inositol derivatives bearing selectively protected hydroxyl groups are relevant precursors of high-value myo-inositols. In the present study, we applied the response surface method to the optimization of kinetic resolution of (±)-1,3,6-tri-O-benzyl-my

Kinetic resolution of a precursor for myo-inositol phosphates under continuous flow conditions

In this work, we have investigated the biocatalytic continuous flow process with a packed-bed reactor for the kinetic resolution of (±)-1,3,6-tri-O- benzyl-myo-inositol ((±)-1) by alcoholysis using Novozym 435. Excellent conversions and stereselectivities were attained in short reaction time. We found that this enzymatic transformation under continuous flow in TBME with vinyl acetate (10:1 ratio with (±)-1) at 50°C, with a 3 min-residence time secured the best results (50% conversion and eep > 99%). The feasibility of a continuous operation of the Novozym 435-containing-packed-bed reactor over a longer period of time was demonstrated via a 9-cycle experiment wherein the lipase remained stable.

On the kinetic resolution of sterically hindered myo-inositol derivatives in organic media by lipases

Sterically hindered myo-inositol derivatives were assayed against different commercial lipases. It was found that dl-1,3,6-tri-O-benzyl-myo-inositol undergoes efficient kinetic resolutions mediated by Pseudomonas sp. lipases (PS-C, PS-IM) and CaLB (Novozy