Literature DB >> 9177298

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

R Sharma1, R M Vohra.   

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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Year:  1997        PMID: 9177298     DOI: 10.1006/bbrc.1997.6659

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Cyclic-imide-hydrolyzing activity of D-hydantoinase from Blastobacter sp. strain A17p-4.

Authors:  C L Soong; J Ogawa; M Honda; S Shimizu
Journal:  Appl Environ Microbiol       Date:  1999-04       Impact factor: 4.792

  1 in total

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