Sharma, R and Vohra, R M (1997) A thermostable D-hydantoinase isolated from a mesophilic Bacillus sp.AR9. Biochemical and biophysical research communications, 234 (2). pp. 485-8. ISSN 0006-291X
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Abstract
A thermostable hydantoinase has been characterized from a mesophilic Bacillus sp.AR9. The hydantoinase produced by this Bacillus sp.AR9 is strictly D-specific and is constitutively produced with high yields (4500 U/ml) in this strain. The enzyme is not only alkalo- and thermostable but has a pH and temperature optimum of 9.5 and 65 degrees C, respectively, which is advantageous for the bioconversion of DL-5-monosubstituted-hydantoin derivatives. The enzyme has a half life of 80 minutes at 70 degrees C and loses only 33% of its activity in 4 hr at 60 degrees C. The enzyme has a broad substrate specificity with a maximum of 100% with hydantoin and about 26% with dihydrouracil. Co+ + ions enhance the activity of the enzyme by more than 60%.
Item Type: | Article |
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Additional Information: | Copyright of this article belongs to Elsevier Science/Academic Press |
Subjects: | Q Science > QD Chemistry |
Depositing User: | Dr. K.P.S.Sengar |
Date Deposited: | 16 Dec 2011 08:55 |
Last Modified: | 27 Mar 2014 05:51 |
URI: | http://crdd.osdd.net/open/id/eprint/369 |
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