Purification and Characterization of Leucine Aminopeptidase from Marine Labyrinthulid Strain 00-Bat-05
-
- Md. Iftekharul Wahid
- The United Graduate School of Agricultural Sciences, Kagoshima University
-
- Yoshikawa Takeshi
- Laboratory of Microbiology, Faculty of Fisheries, Kagoshima University
-
- Sakata Taizo
- Laboratory of Microbiology, Faculty of Fisheries, Kagoshima University
Bibliographic Information
- Other Title
-
- 海産ラビリンチュラ分離株00-Bat-05からのロイシンアミノペプチダーゼの精製と酵素学的性状
Search this article
Abstract
Leucine aminopeptidase (LAP) from marine labyrinthulid strain 00-Bat-05 cells were purified and characterized by enzymological properties. The optimum temperature and pH of LAP from strain 00-Bat-05 was 37°C and pH 8.0, respectively. The thermostability of the enzyme was indicated by remaining 80% of maximum activity after heat treatment at 60°C for 10 min. The enzyme were inactivated by p-chloromercuribenzoic acid (PCMB), 1,10-phenanthroline, bestatin and sodium dodecyl sulphate (SDS), suggesting that it is SH-aminopeptidase. The enzyme activity of LAP was stimulated by Co2+ and inhibited by Zn2+. LAP of 00-Bat-05 had a high specificity for L-leucine-p-nitroanilide among p-nitroanilide derivatives of L-amino acids tested.
Journal
-
- Aquaculture Science
-
Aquaculture Science 56 (1), 1-8, 2008
Japanese Society for Aquaculture Science
- Tweet
Details 詳細情報について
-
- CRID
- 1390001204716290304
-
- NII Article ID
- 10026138894
-
- NII Book ID
- AN00124667
-
- ISSN
- 21850194
- 03714217
-
- NDL BIB ID
- 9427299
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- IRDB
- NDL
- CiNii Articles
-
- Abstract License Flag
- Disallowed