Rui Yamaguchi
   Department   Kumamoto Health Science University  Department of Medical Technology, Faculty of Health Science
   Kumamoto Health Science University Graduate School  Division of Health Sciences, Graduate School of Health Sciences
   Position   Associate Professor
Language English
Publication Date 2012/03
Type
Peer Review Peer reviewed
Title Effects of salt and ligand concentrations on the thermal unfolding and refolding of halophilic starch-binding domain from Kocuria varians alpha-amylase.
Contribution Type
Journal Protein Pept Lett.
Journal TypeAnother Country
Volume, Issue, Page 19,pp.326-332
Total page number 6
Authorship Lead author
Author and coauthor Yamaguchi R, Arakawa T, Tokunaga H, Ishibashi M, Tokunaga M
Details The starch binding domain of α-amlylase from moderate halophile was expressed in E. coli with His tag (His- SBD12) and characterized for its halophilic properties. His-SBD12 was stable up to 35°C and showed binding activity, although at reduced level, to amylose even in the absence of NaCl. Both NaCl and specific ligands exhibited insignificant influence on the secondary structure of His-SBD12, but showed significant stabilization effects against thermal unfolding concentration-dependently, showing its halophilic properties.