First example of hydrolytic kinetic resolution of acrylate of secondary alcohols by lipase Amano AK

• Published in: Journal of molecular catalysis. B, Enzymatic Vol. 72; no. 3; pp. 270 - 275
• Main Authors: Bora, Pranjal P., Bez, Ghanashyam, Anal, Jasha Momo H.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.11.2011; Elsevier
• Subjects: Acrylates; Alcohol; Aqueous; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Enantioselective; Fundamental and applied biological sciences. Psychology; Lipase; Methods. Procedures. Technologies; Acrylates; Alcohol; Enantioselective; Aqueous; Lipase; Separation; Enantioselectivity; Enzyme; Triacylglycerol lipase; Esterases; Carboxylic ester hydrolases; Hydrolysis; Enantiomer; Hydrolases; Secondary alcohol
• ISSN: 1381-1177; 1873-3158
• DOI: 10.1016/j.molcatb.2011.06.015

[Display omitted] ► First report on lipase catalyzed hydrolytic kinetic resolution of acrylates of secondary alcohols. ► In this study, it is established that lipase Amano AK catalyzes hydrolysis of acrylates of secondary alcohol at pH 7.0. ► The method gives very good enantioselectivity. ► As the enzymatic reactions address numerous environmental concerns, the method is advantageous to homogeneous organometallic catalysis and organocatalysis. ► The applicability of the method is shown for stereoselective synthesis of ( R)-5-Butyl-2( 5H)-furanone, a lactone using Ring Closing Metathesis (RCM) strategy. Lipase Amano AK is found to be extremely efficient catalyst for hydrolytic kinetic resolution of acrylates of secondary alcohols in aqueous phosphate buffer at pH 7.0. Both aliphatic and benzylic secondary alcohols show good to excellent E values.