Preparation and properties of Clostridium thermocellum lichenase deletion variants and their use for construction of bifunctional hybrid proteins

Major properties (pH and temperature optimum, stability) of lichenase (beta -1,3-1,4-glucanase) deletion variants from Clostridium thermocellum were c omparatively studied. The deletion variant LicBM2 was used to create hybrid bifunctional proteins by fusion with sequences of the green fluorescent pr otein (GFP) from Aequorea victoria. The data show that in hybrid proteins b oth GFP and lichenase retain their major properties, namely, GFP remains a fluorescent protein and the lichenase retains activity and high thermostabi lity. Based on the results of this investigation and results that have been obtained earlier, the use of the deletion variants of lichenase and the bi functional hybrid proteins as reporter proteins is suggested.