The properties of immobilized caldolysin, a thermostable protease from an extreme thermophile

✍ Scribed by Donald A. Cowan; Roy M. Daniel

• Publisher: John Wiley and Sons
• Year: 1982
• Tongue: English
• Weight: 422 KB
• Volume: 24
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260240912

✦ Synopsis

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 occurred on immobilization (26, 69, and 89%). The pH optimum of both CM‐cellulose and CPG‐immobilized Caldolysin was decreased by about one pH unit. The K~m~ for Sepharose‐Caldolysin was unchanged with respect to the free protease, while those for CM‐cellulose‐Caldolysin and CPG‐Caldolysin were lower by approximately one order of magnitude. Immobilization to both Sepharose and CM‐cellulose increased the thermostability of Caldolysin at high temperatures, while CPG‐Caldolysin was less thermostable than the free protease.