Fast multipoint immobilization of lipase through chiral L-proline on a MOF as a chiral bioreactor.

Affiliation

Lirio S(1), Shih YH(1), So PB(1), Liu LH(1), Yen YT(1), Furukawa S(2), Liu WL(3), Huang HY(1), Lin CH(4).
Author information:
(1)Department of Chemistry, Chung Yuan Christian University, No. 200, Zhongbei Rd., Zhongli Dist., Taoyuan 32023, Taiwan.
(2)Institute for Integrated Cell-Material Sciences
(WPI-iCeMS), Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.
(3)College of Science, Chung Yuan Christian University, No. 200, Zhongbei Rd., Zhongli Dist., Taoyuan 32023, Taiwan.
(4)Department of Chemistry, National Taiwan Normal University, National Taiwan Normal University, No. 88, Sec. 4, Ting-Chow Rd., Taipei, 11676, Taiwan. [Email]

Abstract

In this paper, we describe the facile preparation of a chiral catalyst by the combination of the amino acid, l-proline (Pro), and the enzyme, porcine pancreas lipase (PPL), immobilized on a microporous metal-organic framework (PPL-Pro@MOF). The multipoint immobilization of PPL onto the MOF is made possible with the aid of Pro, which also provided a chiral environment for enhanced enantioselectivity. The application of the microporous MOF is pivotal in maintaining the catalytic activity of PPL, wherein it prevented the leaching of Pro during the catalytic reaction, leading to the enhanced activity of PPL. The prepared biocatalyst was applied in asymmetric carbon-carbon bond formation, demonstrating the potential of this simple approach for chemical transformations.