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. 1997 May 19;234(2):485-8.
doi: 10.1006/bbrc.1997.6659.

A thermostable D-hydantoinase isolated from a mesophilic Bacillus sp.AR9

R Sharma  1 , R M Vohra
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A thermostable D-hydantoinase isolated from a mesophilic Bacillus sp.AR9

R Sharma et al. Biochem Biophys Res Commun. .

Erratum in

  • Biochem Biophys Res Commun 1997 Aug 28;237(3):759

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%.

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