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Co-expression of the recombined alcohol dehydrogenase and glucose dehydrogenase and cross-linked enzyme aggregates stabilization.

Abstract：

:As the key chiral precursor of Crizotinib (S)-1-(2,6-dichloro-3-fluorophenyl) phenethyl alcohol can be prepared from 1-(2,6-dichloro-3-fluorophenyl) acetophenone by the reductive coupling reactions of alcohol dehydrogenase (ADH) and glucose dehydrogenases (GDH). In this work the heterologous expression plasmids harbouring the encoding genes of ADH and GDH were constructed respectively and co-expressed in the same E. coli strain. After optimization, a co-cross-linked enzyme aggregates (co-CLEAs) of both ADH and GDH were prepared from crude enzyme extracts by cross-linking with the mass ratio of Tween 80, glutaraldehyde and total protein (0.6:1:2) which rendered immobilized biocatalysts that retained 81.90% (ADH) and 40.29% (GDH) activity retention. The ADH/GDH co-CLEAs show increased thermal stability and pH stability compared to both enzymes. The ADH/GDH co-CLEAs also show 80% (ADH) and 87% (GDH) residual activity after seven cycles of repeated use. These results make the ADH/GDH co-CLEAs a potential biocatalyst for the industrial preparation of (S)-1-(2,6-dichloro-3-fluorophenyl) phenethyl alcohol.

journal_name

Bioresour Technol

journal_title

Bioresource technology

authors

Hu X,Liu L,Chen D,Wang Y,Zhang J,Shao L

doi

10.1016/j.biortech.2016.10.076

subject

Has Abstract

pub_date

2017-01-01 00:00:00

pages

531-535

eissn

0960-8524

issn

1873-2976

pii

S0960-8524(16)31490-0

journal_volume

224

pub_type

杂志文章

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