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Stability of Thermostable Enzyme, Aqualysin I ; a Subtilisin-type Serine Protease fromThermus aquaticusYT-1

Terumichi Tanaka, Hiroshi Matsuzawa, Takahisa Ohta

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Abstract

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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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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Available abstract

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.

Key concepts: Thermus aquaticus, Subtilisin, Thermus, Enzyme, Serine protease, Thermophile, Biochemistry, Protease

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Stability of Thermostable Enzyme, Aqualysin I ; a Subtilisin-type Serine Protease fromThermus aquaticusYT-1 — Research Paper | ScholarLens