期刊
APPLIED CATALYSIS A-GENERAL
卷 609, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.apcata.2020.117909
关键词
Alcohol dehydrogenase; Biotransformation; Enzyme catalysis; Enzyme immobilization; Statin precursor synthesis
资金
- European Union project ROBOX under EU's Horizon 2020 Programme Research and Innovation actions H2020-LEIT BIO-2014-1 [635734]
- COST Action [CM 1303]
- Purolite Life Sciences(R)
- UAB
- European Union [665919]
Statins inhibit the synthesis of LDL-cholesterol related to cardiovascular diseases. ADH99 and NOX are used for the oxidation of chlorolactol to chlorolactone, leading to improved reaction yield and efficiency.
Statins inhibit the synthesis of LDL-cholesterol which is related to cardiovascular diseases. One of the key steps in the synthesis of the chiral side chain of some statins is the oxidation of the chlorolactol to chlorolactone. This oxidation has been performed by an alcohol dehydrogenase (ADH99) using a NADPH-oxidase (NOX) as a cofactor regeneration system. The reaction conditions were optimised obtaining high reaction yield (94.7 %), space time yield (4.6 g L-1 h(-1)) and biocatalyst yield (7.9 mg product mg(-1) biocatalyst). Both enzymes have been efficiently immobilised onto different supports (Eupergit (R) CM, Amino-agarose, Epoxy agarose-UAB, Purolite ECR8409 and ECR8415). ADH99 showed a stability improvement when immobilised. However, NOX did not show any significant stability enhancement. The most stable ADH99 immobilised derivative, ADH99-Epoxy agarose-UAB, was used to perform the oxidation, improving 1.5-fold both, the total amount of product produced and the biocatalyst yield compared to the ADH99 soluble form.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据