Skip Navigation

Journal of Biochemistry 2006 139(6):1065-1071; doi:10.1093/jb/mvj106
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Morimoto, K.
Right arrow Articles by Inouye, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Morimoto, K.
Right arrow Articles by Inouye, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

Regular Paper

Effects of High Concentration of Salts on the Esterase Activity and Structure of a Kiwifruit Peptidase, Actinidain

Koichi Morimoto1, Erino Furuta1, Hiroshi Hashimoto1 and Kuniyo Inouye2,*

1 Department of Biotechnological Science, Kinki University, Nishimitani, Kinokawa, Wakayama 649-6493; and 2 Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502

* To whom correspondence should be addressed. Tel: +81-75-753-6266, Fax: +81-75-753-6265, E-mail: inouye{at}kais.kyoto-u.ac.jp

Effects of salts on the activity and stability of actinidain were examined. With increasing salt concentration up to 0.5 M, the activity (kcat/Km) for N-{alpha}-Cbz-L-lysine p-nitrophenyl ester decreased to 40% of that in the absence of salt. The inhibitor constant Ki of LiCl, NaCl, and KCl was 0.16–0.43 M. With 3 M KCl and NaCl, the specificity constant kcat/Km recovered to 110 and 75%, respectively. No re-activation was observed with LiCl. The inhibition and re-activation were dependent on the changes in both Km and kcat, whereas no CD change was observed. The tryptophan fluorescence of actinidain was not affected by 0–0.5 M salt, but a considerable decrease in its intensity was observed with increasing salt concentration from 0.5 to 3.0 M. These results suggest that the inhibition observed with the lower salt concentration (<0.5 M) is due to attenuation of the electrostatic interaction between the enzyme and substrate, and the higher concentration (0.5–3.0 M) induces structural change in the states of tryptophan residues, which is associated with the re-activation. Actinidain keeps considerably high activity and stability even in the presence of 3 M salts.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
K. Morimoto, K. Kawabata, S. Kunii, K. Hamano, T. Saito, and B. Tonomura
Characterization of Type I Collagen Fibril Formation Using Thioflavin T Fluorescent Dye
J. Biochem., May 1, 2009; 145(5): 677 - 684.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
C. Tatsumi, Y. Hashida, K. Yasukawa, and K. Inouye
Effects of Site-directed Mutagenesis of the Surface Residues Gln128 and Gln225 of Thermolysin on its Catalytic Activity
J. Biochem., June 1, 2007; 141(6): 835 - 842.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.