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Catalytic properties and potential of an extracellular protease from an extreme halophile

✍ Scribed by Keungarp Ryu; Jungbae Kim; Jonathan S. Dordick

Book ID
103530296
Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
850 KB
Volume
16
Category
Article
ISSN
0141-0229

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An extracellular protease has been purified to how to improve conventional enzymes for catalysis from the extreme halophile, Halobacterium halobium. under harsh conditions as well as to increase dramati- The irreversible inactivation kinetics of this halophilic procally the repertoire of enzymatic

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## Abstract Caldolysin, the extracellular thermostable metal‐chelator‐sensitive lytic protease from __Thermus__ T‐351 was immobilized to Sepharose 4B, CM‐cellulose, and controlled pore glass (CPG). Although protein binding efficiencies were high (96, 88, and 95%), some loss of enzyme activity occur