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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.    Conclusion  We successfully produced a large amount of tetrameric streptavidin as a secretory-form protein with unique thermotolerance.    Electronic supplementary material  The online version of this article (doi:10.1186/s12934-014-0188-y) contains supplementary material, which is available to authorized users.

Secretory production of tetrameric native full-length streptavidin with thermostability using Streptomyces lividans as a host