Purification and some properties of a protease from Streptomyces limosus.

Article abstract of DOI:10.1271/bbb.59.474

Streptomyces limosus was selected because it secreted a novel protease that catalyzed the synthetic reaction forming Pro-Pro-Pro from Pro-Pro. The protease was purified to an electrophoretically homogeneous state and an activity of more than about 20,000-fold that of the culture broth. The molecular mass of the enzyme was estimated to be 50 kDa by SDS-polyacrylamide gel electrophoresis. The enzyme was most active in alkaline pH for the synthetic reaction producing Pro-Pro-Pro from Pro-Pro, although for the hydrolytic reaction forming proline it was most active in neutral pH. The enzyme was inhibited by 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP) and diazoacetyl-DL-norleucine methyl ester (DAN). It can be considered that this enzyme belongs to the class of aspartic proteases. The substrate specificity indicates that this enzyme has a strong affinity for proline as a N-terminal amino acid of peptides.

Full text of DOI:10.1271/bbb.59.474

This article was downloaded by: [Thomas Jefferson University]
On: 21 December 2014, At: 13:38
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
Purification and Some Properties of a Protease from
Streptomyces limosus
Tetsuo Muroa, Yomi Watanabea, Akio Sugiharaa, Yuji Shimadaa, Toshihiro Nagaoa,
Shigeyuki Takenishia & Yoshio Tominagaa
a Osaka Municipal Technical Research Institute, 6–50 Morinomiya 1-chome, Joto-ku,
Osaka 536, Japan
Published online: 12 Jun 2014.
To cite this article: Tetsuo Muro, Yomi Watanabe, Akio Sugihara, Yuji Shimada, Toshihiro Nagao, Shigeyuki Takenishi
& Yoshio Tominaga (1995) Purification and Some Properties of a Protease from Streptomyces limosus, Bioscience,
Biotechnology, and Biochemistry, 59:3, 474-478, DOI: 10.1271/bbb.59.474
To link to this article: http://dx.doi.org/10.1271/bbb.59.474
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

NII-Electronic Library Service

NII-Electronic Library Service

NII-Electronic Library Service

NII-Electronic Library Service

NII-Electronic Library Service