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Home >> Industrial and Microbial Biotechnology >> Protein and Enzymes Engineering >>Artificial Random Mutagenesis

Artificial Random Mutagenesis
Following are some examples of enzyme engineering through mutations (information on this subject is also available on line <http://www.che.caltech. edu:80/groups/fha/enzyme/directed.html>). Other examples can be found in several reviews published during 1999-2000. (i) Enantioselectivity was evolved in a naturally occurring lipase, which had no selectivity for hydrolysis of racemic 2-methyldecanoic ester.
Through several rounds of mutagenesis, an enzyme was evolved that catalysed the reaction at more then 90% enantiomeric excess. (ii) Enantioselectivity of a hydantoinase was inverted through mutations and screening, so that it preferred L- over D-5 (2-methylthioethyl) hydantoin with five fold increased activity.
This will be used for industrial production of L-methionine. (iii) An aspartate transaminase has been evolved due to alterations in active site, so that it had 2.6 x art 106- fold higher activity towards an entirely new substrate, valine.

 

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