کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
34730 | 45042 | 2013 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: His-tagged Horse Liver Alcohol Dehydrogenase: Immobilization and application in the bio-based enantioselective synthesis of (S)-arylpropanols His-tagged Horse Liver Alcohol Dehydrogenase: Immobilization and application in the bio-based enantioselective synthesis of (S)-arylpropanols](/preview/png/34730.png)
• Immobilization of His-tagged HLADH was successfully reported.
• Effect of pH, temperature and organic co-solvents was investigated.
• Application of the new imm-His-HLADH on the reduction of aldehydes was investigated.
• Chemoenzymatic synthesis of enantiopure Profenols via DKR with His-HLADH was reported.
The novel histidine-tagged Horse Liver Alcohol Dehydrogenase (His-HLADH-EE) was successfully purified and covalently immobilized onto a solid support in a one-step procedure through a metal-directed technique. A full characterization of the immobilized enzyme was carried out. Effects of pH, temperature and organic co-solvents were deeply investigated and they showed a shift in the optimum pH with respect to the free form as well as increased stability to temperature and solvents. The immobilized His-HLADH-EE proved to be effective as catalyst in the reduction of aliphatic and aromatic aldehydes. Application of the free and immobilized His-HLADH-EE to the chemo-enzymatic synthesis of (S)-Profenols demonstrated enhanced enantioselectivity and high reusability of the immobilized form. The achievement of a robust and effective immobilization of an alcohol dehydrogenase substantiated the use of biocatalytic reduction in the synthesis of primary alcohols and valuable chiral intermediates especially for pharmaceutical industries.
Journal: Process Biochemistry - Volume 48, Issues 5–6, May–June 2013, Pages 810–818