Characterization of D-aminoacylase from Alcaligenes denitrificans DA181.

Article abstract of DOI:10.1271/bbb.56.1392

The D-aminoacylase produced by Alcaligenes denitrificans DA181 was a new type of aminoacylase which had both high stereospecificity and specific activity. The molecular weight and isoelectric point of this enzyme were 58,000 and 4.4, respectively. The apparent Km and kcat values of this enzyme for N-acetyl-D-methionine were estimated to be 0.48 mM and 6.24 x 10(4) min-1, respectively. The optimum temperature was 45 degrees C. The enzyme was stable up to 55 degrees C for 1 hr in the presence of 0.2 mg/ml bovine serum albumin. The enzyme was stable in the pH range of 6.0 to 11.0 with an optimum pH of 7.5. This enzyme contained about 2.1 g atom of zinc per mole of enzyme. Enzyme activity was inhibited by incubation with EDTA. The inhibition by EDTA was fully reversed by Co2+ and partially by Zn2+.

Full text of DOI:10.1271/bbb.56.1392

Evaluation Only. Created with Aspose.PDF. Copyright 2002-2021 Aspose Pty Ltd.
This article was downloaded by: [University of Strathclyde]
On: 26 November 2014, At: 04:01
Publisher: Taylor & Francis
Informa Ltd Registered in England and Wales Registered Number: 1072954 Registered office: Mortimer
House, 37-41 Mortimer Street, London W1T 3JH, UK
Bioscience, Biotechnology, and Biochemistry
Publication details, including instructions for authors and subscription information:
http://www.tandfonline.com/loi/tbbb20
Characterization of D-Aminoacylase from Alcaligenes
denitrificans DA181
Yunn-Bor Yanga, Kuang-Ming Hsiaoa, Hung-Lia, Hiroyuki Yanoab, Akira Tsugitaab & Ying-
Chieh Tsaia
a Institute of Biochemistry, National Yang-Ming Medical College, Taipei, Taiwan 11221,
R.O.C.
b Life Science Institute, Science University of Tokyo, Noda, Chiba 278, Japan
Published online: 12 Jun 2014.
To cite this article: Yunn-Bor Yang, Kuang-Ming Hsiao, Hung-Li, Hiroyuki Yano, Akira Tsugita & Ying-Chieh Tsai (1992)
Characterization of D-Aminoacylase from Alcaligenes denitrificans DA181, Bioscience, Biotechnology, and Biochemistry,
56:9, 1392-1395, DOI: 10.1271/bbb.56.1392
To link to this article: http://dx.doi.org/10.1271/bbb.56.1392
PLEASE SCROLL DOWN FOR ARTICLE
Taylor & Francis makes every effort to ensure the accuracy of all the information (the “Content”) contained
in the publications on our platform. However, Taylor & Francis, our agents, and our licensors make no
representations or warranties whatsoever as to the accuracy, completeness, or suitability for any purpose of
the Content. Any opinions and views expressed in this publication are the opinions and views of the authors,
and are not the views of or endorsed by Taylor & Francis. The accuracy of the Content should not be relied
upon and should be independently verified with primary sources of information. Taylor and Francis shall
not be liable for any losses, actions, claims, proceedings, demands, costs, expenses, damages, and other
liabilities whatsoever or howsoever caused arising directly or indirectly in connection with, in relation to or
arising out of the use of the Content.
This article may be used for research, teaching, and private study purposes. Any substantial or systematic
reproduction, redistribution, reselling, loan, sub-licensing, systematic supply, or distribution in any
form to anyone is expressly forbidden. Terms & Conditions of access and use can be found at http://
www.tandfonline.com/page/terms-and-conditions

Evaluation Only. Created with Aspose.PDF. Copyright 2002-2021 Aspose Pty Ltd.
NII-Electronic Library Service

Evaluation Only. Created with Aspose.PDF. Copyright 2002-2021 Aspose Pty Ltd.
NII-Electronic Library Service

Evaluation Only. Created with Aspose.PDF. Copyright 2002-2021 Aspose Pty Ltd.
NII-Electronic Library Service