Kinetic resolution of 1,2-diols using immobilized Burkholderia cepacia lipase: A combined experimental and molecular dynamics investigation.

Kinetic resolution of rac-1,2-diols using the biocatalyst Burkholderia cepacia lipase (BCL) immobilized on a biodegradable binary blend support of hydroxypropyl methyl cellulose(HPMC)/polyvinyl alcohol (PVA) has been investigated. The immobilization technique improved enzyme activity significantly and it has excellent recyclability with good yield and enantiomeric excess values up to the studied range of nine cycles. At optimum reaction conditions, conversion of 45-50% with excellent enantiomeric excess (up to 99% ee) were obtained. It was observed that BCL shows enantio-preference to R form of primary hydroxyl group for acylation, whereas S form is preferred for diacetate formation. The resultant products were characterized with the help of different analytical techniques such as