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Stability of Cytochrome P‐450 Enzyme and the Dehalogenation Activity in Resting Cultures of Pseudomonas putida PpG 786
Author(s) -
Vilker Vincent L.,
Khan Fatima
Publication year - 1989
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 - 10.1002/btpr.5420050208
Subject(s) - pseudomonas putida , halogenation , substrate (aquarium) , cytochrome , enzyme , chemistry , enzyme assay , pseudomonadales , intracellular , pseudomonadaceae , biochemistry , bacteria , pseudomonas , chromatography , biology , organic chemistry , ecology , genetics
The activity of resting cultures of P. putida PpG 786 for dehalogenating trace levels of the substrate 1,2‐dibromo‐3‐chloropropane (DBCP) was examined as a function of the intracellular concentration of the enzyme cytochrome P‐450 cam monooxygenase. The stability of both the intracellular enzyme concentration and dehalogenation activity were shown to decline when the resting cultures were aged up to 48 hours at room temperature. Activity was retained when the cultures were aged to 48 hours at refrigeration temperatures. Dehalogenation activity did not correlate as well with cell viability as with enzyme concentration. DBCP toxicity toward the bacteria was present over the entire substrate concentration range that was investigated, and at about one millimolar initial DBCP concentration, dehalogenation activity was almost completely lost.