z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom