1112-33-0

Usage

InChI:InChI=1/C6H12O4/c1-6(2,3-7)4(8)5(9)10/h4,7-8H,3H2,1-2H3,(H,9,10)/t4-/m0/s1

Upstream product

• 597-31-9 2,2-dimethyl-3-hydroxypropionaldehyde 
• 79-50-5 pantolactone 
• 102096-61-7 (R)-pantolactone (1S,2S,4S)-bicyclo<2.2.1>hept-5-ene-2-carboxylate 

Downstream Products

• 79-83-4 pantothenic acid 
• 599-04-2 (R)-Pantolacton 
• 1613372-38-5 C₅₃H₆₅N₇O₁₀ 
• 1616962-62-9 C₂₉H₂₈N₂O₁₀ 
• 1613372-35-2 C₃₉H₅₀N₂O₁₀Si 
• 1613372-30-7 C₄₁H₅₃ClN₄O₁₀S₂Si 
• 1613372-29-4 C₃₉H₅₂N₄O₉S₂Si 
• 1613372-28-3 C₄₄H₆₀N₄O₁₁S₂Si 
• 1613372-27-2 C₃₂H₃₇NO₉Si 
• 1613372-26-1 C₃₆H₄₅NO₉Si 

Relevant academic research and scientific papers

Preparation method of hydroxyaldehyde and method for resolving optical isomer by using electrodialysis technology

The present invention provides a process for preparing hydroxyaldehydes using an immobilized catalyst, wherein the immobilized catalyst comprises a solid support and a tertiary amine-based functionalgroup. The invention also provides a method for preparing a polyhydroxy alcohol compound and a polyhydroxy acid compound. The invention further provides a method for splitting the optical isomer fromthe raceme through electrodialysis.

Development of a Novel Biocatalyst for the Resolution of rac-Pantolactone

A novel L-pantolactone hydrolase, Lph, from Agrobacterium tumefaciens Lu681 was characterized, which stereospecifically hydrolyses L-pantolactone to L-pantoic acid yielding D-pantolactone with > 95% enantiomeric excess. The enzyme was found to be a 30 kDa-Zn2+-hydrolase with a Km for L-pantolactone of 7 mM and a Vmax of 30 U/mg. The corresponding lph gene was identified as an 807 bp ORF and cloned into E. coli. It was overexpressed under control of Ptac and Prha yielding enzyme activities of up to 600 U/g dry weight. Resolution of D,L-pantolactone in repeated batches with isolated Lph and enzyme recovery by membrane filtration gave D-pantolactone with 50% yield and 90-95% ee over 6 days. Covalent immobilization to EupergitC led to a stable biocatalyst easy to handle in a repeated batch production of D-pantolactone. Further improvements in the activity of Lph were achieved by directed evolution of the enzyme. Activities of mutants F62S, K197D and F100L were increased 2.3, 1.7, and 1.5 fold, respectively.

A convenient practical method for the preparation of ( - )-(1S,2S)-5-norbornene-2-carboxylic acid, incorporating efficient recovery of the chiral auxiliary D-pantolactone

A convenient practical method was developed for the preparation of enantiomerically pure ( - )-(1S,2S)-5-norbornene-2-carboxylic acid, wherein the chiral auxiliary D-pantolactone was recovered efficiently.