@article{open369,
          volume = {234},
          number = {2},
           month = {May},
          author = {R Sharma and R M Vohra},
            note = {Copyright of this article belongs to Elsevier Science/Academic Press},
           title = {A thermostable D-hydantoinase isolated from a mesophilic Bacillus sp.AR9.},
       publisher = {Elsevier Science/Academic Press},
            year = {1997},
         journal = {Biochemical and biophysical research communications},
           pages = {485--8},
             url = {http://crdd.osdd.net/open/369/},
        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\%.}
}