Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations

نویسندگان

  • S. Leuchs
  • L. Greiner
چکیده

The alcohol dehydrogenase from Lactobacillus brevis (LbADH) is a versatile catalyst for enantioselective reduction of ketones. Its substrate scope is wide with high regioand enantioselectivity. In this critical review, we have gathered the information available on the substrate scope as well as the applications reported. Quantitative information such as productivity per catalyst, space-time yield (STY), cofactor utilisation, and stability are derived to allow comparison and assessment of practical value.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Optimization of enzymatic gas-phase reactions by increasing the long-term stability of the catalyst.

Enzymatic gas-phase reactions are usually performed in continuous reactors, and thus very stable and active catalysts are required to perform such transformations on cost-effective levels. The present work is concerned with the reduction of gaseous acetophenone to enantiomerically pure (R)-1-phenylethanol catalyzed by solid alcohol dehydrogenase from Lactobacillus brevis (LBADH), immobilized on...

متن کامل

Steric vs. electronic effects in the Lactobacillus brevis ADH-catalyzed bioreduction of ketones.

Lactobacillus brevis ADH (LBADH) is an alcohol dehydrogenase that is commonly employed to reduce alkyl or aryl ketones usually bearing a methyl, an ethyl or a chloromethyl as a small ketone substituent to the corresponding (R)-alcohols. Herein we have tested a series of 24 acetophenone derivatives differing in their size and electronic properties for their reduction employing LBADH. After plott...

متن کامل

Stable Continuous Operation of a Biphasic Enantioselective Enzymatic Reduction

Continuous operation of alcohol dehydrogenase (ADH) catalysed enantioselective reduction in a biphasic sytem showed gains in productivity and stability of the overall reaction system. The total turnover numbers obtained for the cofactor NADP + are high with up to 1.5 10 4 . Productivity for (R)-2-butanol with Lactobacillus brevis ADH was up to 26 kmol (mol enzyme) 1 . Enantioselectivity was gre...

متن کامل

Purification and gene cloning of a dehydrogenase from Lactobacillus brevis that catalyzes a reaction involved in aflatoxin biosynthesis.

When 10 strains of lactic acid bacteria were incubated with 5'-hydroxyaverantin (HAVN), a precursor of aflatoxins, seven of them converted HAVN to averufin; the same reaction is found in aflatoxin biosynthesis of aflatoxigenic fungi. These bacteria had a dehydrogenase that catalyzed the reaction from HAVN to 5'-oxoaverantin (OAVN), which was so unstable that it was easily converted to averufin....

متن کامل

Cloning, expression, purification, and analysis of mannitol dehydrogenase gene mtlK from Lactobacillus brevis.

The commercial production of mannitol involves high-pressure hydrogenation of fructose using a nickel catalyst, a costly process. Mannitol can be produced through fermentation by microorganisms. Currently, a few Lactobacillus strains are used to develop an efficient process for mannitol bioproduction; most of the strains produce mannitol from fructose with other products. An approach toward imp...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2011