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Surface display of bacterial tyrosinase on spores of Bacillus subtilis using CotE as an anchor protein
Author(s) -
HosseiniAbari Afrouzossadat,
Kim ByungGee,
Lee SangHyuk,
Emtiazi Giti,
Kim Wooil,
Kim JuneHyung
Publication year - 2016
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201600203
Subject(s) - tyrosinase , spore , bacillus subtilis , bacillus megaterium , chemistry , biochemistry , enzyme , substrate (aquarium) , biology , microbiology and biotechnology , bacteria , ecology , genetics
Tyrosinases, copper‐containing monooxygenases, are widely used enzymes for industrial, medical, and environmental applications. We report the first functional surface display of Bacillus megaterium tyrosinase on Bacillus subtilis spores using CotE as an anchor protein. Flow Cytometry was used to verify surface expression of tyrosinase on the purified spores. Moreover, tyrosinase activity of the displayed enzyme on B. subtilis spores was monitored in the presence of L‐tyrosine (substrate) and CuSO 4 (inducer). The stability of the spore‐displayed tyrosinase was then evaluated after 15 days maintenance of the spores at room temperature, and no significant decrease in the enzyme activity was observed. In addition, the tyrosinase‐expressing spores could be repeatedly used with 62% retained enzymatic activity after six times washing with Tris‐HCl buffer. This genetically immobilized tyrosinase on the spores would make a new advance in industrial, medical, and environmental applications.