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3 results about "Halohydrin dehalogenase" patented technology

A halohydrin dehalogenase is an enzyme involved in the bacterial degradation of vicinal halohydrins. In several species of bacteria, it catalyses the dehalogenation of halohydrins to produce the corresponding epoxides. Different isoforms of the enzyme fall into one of three groups, A, B or C. Halogenases of the same class are genetically similar, but differ greatly from halogenases from a different group. Currently the most well-studied isoform is HheC which is purified from the bacterial species Agrobacterium radiobacter. The ability to dehalogenate organic compounds as well as form enantiomeric selective epoxides have generated interest in the potential of this enzyme in the biochemical field.

Method for improving biosynthesis efficiency of epichlorohydrin

The invention discloses a method for improving the biosynthesis efficiency of epichlorohydrin, which utilizes immobilized halohydrin dehalogenase to catalytically synthesize epichlorohydrin, and utilizes modified strong base anion exchange resin to adsorb chloride ions generated in the catalytic synthesis of epichlorohydrin, thereby solving the problem of reaction balance caused by chloride ion accumulation and improving the biosynthesis efficiency of epichlorohydrin. The synthesis efficiency of a target product is improved.
Owner:ZHEJIANG UNIV OF TECH

Halogen alcohol dehalogenase mutant and application thereof in asymmetric synthesis of epsilon-substituted alcohol

PendingCN122326580ADehalogenaseEnantio selectivity
This invention relates to the fields of enzyme engineering and biocatalysis, disclosing a halohydrin dehalogenase mutant and its catalytic enantioselective dehalogenation hydroxylation reaction of a series of racemic ε-halohydrins, preparing corresponding chiral ε-diols and chiral ε-halohydrins. The invention utilizes a fungicide derived from *Agrobacterium radiodurans* (…). Agrobacterium tumefaciens The wild-type haloalcohol dehalogenase HheC (amino acid sequence SEQ ID NO:2) of AD1 was used as the parent enzyme, and was obtained by combining 2 to 6 amino acid site mutations at L142, W249, P84, T134, N176, and F186. The mutant can be used to catalyze the kinetic resolution and dehalogenation reactions of racemic ε-haloalcohols, synthesizing a series of high-optical-purity chiral ε-diols and chiral ε-haloalcohols. These compounds are important chiral building blocks for the preparation of various pharmaceutical chemicals and have broad industrial application value.
Owner:ZUNYI MEDICAL UNIVERSITY

A method for targeted modification to improve the activity of halohydrin dehalogenase

This application discloses a method for targeted modification to improve the activity of halohydrin dehalogenase, belonging to the field of bioengineering technology. The halohydrin dehalogenase mutant obtained by this application is produced by single-point mutation or combination mutation of alanine at position 60 and histidine at position 179 in the sequence shown in SEQ ID NO.1. Compared with the wild-type halohydrin dehalogenase, the mutant obtained in this application shows significantly improved enzyme activity and dehalogenation efficiency in the catalytic preparation of 1-chloro-2-propanol and 2-chloro-1-ethanol. The mutant enzyme activity is increased by 1.78 times, and the dehalogenation efficiency is increased by 77.8%, showing good prospects for industrial application.
Owner:NANTONG WANNIANCHANG PHARMA