Stability of Thermostable Enzyme, Aqualysin I ; a Subtilisin-type Serine Protease fromThermus aquaticusYT-1
Author(s) -
Terumichi TANAKA,
Hiroshi Matsuzawa,
Takahisa Ohta
Publication year - 1998
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.62.1806
Subject(s) - thermus aquaticus , subtilisin , thermus , enzyme , serine protease , thermophile , biochemistry , protease , chemistry , heat stability , biology , materials science , composite material
We characterized the heat stability and detergent stabilities of aqualysin I, produced by Thermus aquaticus YT-1, and compared them with those of fungal proteinase K and Bacillus subtilisin. Aqualysin I displayed excellent heat and detergent stabilities. Proteinase K, another Cys-containing enzyme, was less stable than aqualysin I. All these enzymes maintained activities in the presence of urea or Tween-20.
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