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Operational Stability of High Initial Activity Protease Catalysts in Organic Solvents
Author(s) -
Fernandes João F. Amorim,
Halling Peter J.
Publication year - 2002
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp020098g
Subject(s) - subtilisin , protease , chemistry , adsorption , catalysis , enzyme , aqueous solution , chromatography , chymotrypsin , enzyme assay , specific activity , immobilized enzyme , organic chemistry , trypsin
The first studies on the operational stability of cross‐linked enzyme crystals (CLECs) in organic media are described. Although these catalysts display high initial specific activity, they inactivate rapidly, losing more than 50% of the initial activity within the first 4 h under continuous flow. Furthermore, the inactivation is not reversible when returned to an aqueous medium. The same rapid inactivation occurs with adsorbed protease preparations that show similar high initial specific activity (propanol‐rinsed enzyme preparations (PREPs) of subtilisin and α‐chymotrypsin).