Publications by authors named "Han-Zhong Deng"

Article Synopsis
  • - Chiral epichlorohydrin (ECH) is an important intermediate for making chiral pharmaceuticals, but its synthesis faces challenges due to low optical purity caused by reverse reactions.
  • - This study developed a new strategy involving an engineered enzyme called HheC (mutant E85P) to improve the synthesis of (S)-ECH by slowing down the reverse reactions while maintaining forward reaction efficiency.
  • - The result of this engineering was a significant increase in yield of (S)-ECH to 55.35% and an improvement in optical purity from 92.54% to over 99%, enhancing the potential for green manufacturing of chiral compounds.
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Asymmetric synthesis of chiral epichlorohydrin (ECH) from 1,3-dichloro-2-propanol (1,3-DCP) using halohydrin dehalogenases (HHDHs) is of great value due to the 100% theoretical yield and high enantioselectivity. The vital problem in the asymmetric synthesis is to prepare optically pure ECH. In this study, key amino acid residues located at halide ion channels of HheC (P175S/W249P) (HheC) were modified to regulate the kinetic parameters.

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Asymmetric synthesis of chiral epichlorohydrin (ECH) from 1,3-dichloro-2-propanol (1,3-DCP) using halohydrin dehalogenase (HHDH) is of great value due to the 100% theoretical yield and high enantioselectivity. In this study, HheC (P175S/W249P) was immobilized on an A502Ps resin and used for the preparation of (S)-ECH. In aqueous system, the immobilized HheC catalyzed the biosynthesis of (S)-ECH with 83.

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