title: Secretory production of tetrameric native full-length streptavidin with thermostability using Streptomyces lividans as a host.
abstract: BACKGROUND
  Streptavidin is a tetrameric protein derived from Streptomyces avidinii, and has tight and specific biotin binding affinity. Applications of the streptavidin-biotin system have been widely studied. Streptavidin is generally produced using protein expression in Escherichia coli. In the present study, the secretory production of streptavidin was carried out using Streptomyces lividans as a host.
  
  
  RESULTS
  In this study, we used the gene encoding native full-length streptavidin, whereas the core region is generally used for streptavidin production in E. coli. Tetrameric streptavidin composed of native full-length streptavidin monomers was successfully secreted in the culture supernatant of S. lividans transformants, and had specific biotin binding affinity as strong as streptavidin produced by E. coli. The amount of Sav using S. lividans was about 9 times higher than using E. coli. Surprisingly, streptavidin produced by S. lividans exhibited affinity to biotin after boiling, despite the fact that tetrameric streptavidin is known to lose its biotin binding ability after brief boiling.
  
  
  CONCLUSIONS
  We successfully produced a large amount of tetrameric streptavidin as a secretory-form protein with unique thermotolerance.
authors.affiliation: Biomass Engineering Program, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan. shuhei.noda@riken.jp.
authors.forename: Shuhei
authors.initials: S
authors.lastname: Noda
authors.affiliation: Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Japan. t_matsu@rabbit.kobe-u.ac.jp.
authors.forename: Takuya
authors.initials: T
authors.lastname: Matsumoto
authors.affiliation: Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Japan. tanaka@kitty.kobe-u.ac.jp.
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Tanaka
authors.affiliation: Biomass Engineering Program, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan. akondo@kobe-u.ac.jp.|Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Japan. akondo@kobe-u.ac.jp.
authors.forename: Akihiko
authors.initials: A
authors.lastname: Kondo
mesh_terms: D000595:Amino Acid Sequence; D001710:Biotin / Q000737:chemistry / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010957:Plasmids / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D019809:Streptavidin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D048170:Streptomyces lividans / Q000378:metabolism*; D013696:Temperature
chemical_list: D011994:Recombinant Proteins; D001710:Biotin; D019809:Streptavidin