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Chimeric avidin shows stability against harsh chemical conditions—biochemical analysis and 3D structure
Author(s) -
Määttä Juha A.E.,
EisenbergDomovich Yael,
Nordlund Henri R.,
Hayouka Ruchama,
Kulomaa Markku S.,
Livnah Oded,
Hytönen Vesa P.
Publication year - 2011
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.22962
Subject(s) - avidin , biotinylation , streptavidin , chemistry , isothermal titration calorimetry , biotin , biochemistry , biophysics , biology
Avidin and its bacterial analog streptavidin have been widely used in applications in life sciences. Recently, we described a highly thermostable engineered avidin, called chimeric avidin, which is a hybrid of avidin and avidin‐related protein 4. Here, we report a protocol for pilot‐scale production in E. coli and the X‐ray structure of chimeric avidin. The ligand‐binding properties of chimeric avidin were explored with isothermal titration calorimetry. We found chimeric avidin to be more stable against various harsh organic solvents at elevated temperatures compared to avidin and streptavidin. The properties of chimeric avidin make it a potential tool for new applications in biotechnology. Biotechnol. Bioeng. 2011; 108:481–490. © 2010 Wiley Periodicals, Inc.