Efficient selection for thermostable protease in Thermus thermophilus.
An efficient procedure was established to select for thermostable proteases in an extreme thermophile, Thermus thermophilus. A non-protease-secreting mutant derived from T. thermophilus TH125 was used as host and the expression plasmid for aqualysin I from T. aquaticus YT-1 was constructed as a source of thermostable protease. T. thermophilus cells harboring the recombinant plasmid produced active aqualysin I into the medium and were able to grow on a minimal medium containing milk casein as the sole source of carbon and nitrogen.
Takagi
H
H
Department of Bioscience, Fukui Prefectural University, Japan. hiro@fpu.ac.jp
Suzumura
A
A
Hasuura
Y
Y
Hoshino
T
T
Nakamori
S
S
D003470:Culture Media; D004795:Enzyme Stability; D006361:Heating; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D013824:Thermus / Q000201:enzymology / Q000235:genetics; D016963:Thermus thermophilus / Q000254:growth & development* / Q000378:metabolism
D003470:Culture Media; D011993:Recombinant Fusion Proteins; D012697:Serine Endopeptidases; C055102:aqualysin I