TY - JOUR
AU - Prazeres, Duarte M F
AB - The stability of an oligomeric enzyme, penicillin acylase, was studied in aqueous media. The enzyme was produced by mutant cells of Escherichia coli ATCC 9637, extracted from the periplasmic space by osmotic shock and further purified using a pseudo‐affinity adsorption process. Enzyme stabilisation attempts were performed with salts, alcohols and sugars. The highest levels of retained activity were obtained in the presence of 15% (w/v) ammonium or sodium sulfate. A kinetic model was proposed to describe the inactivation of penicillin acylase, taking into account results obtained in stability assays performed at different temperatures and with different enzyme concentrations. According to this model, the inactivation of penicillin acylase involves an intermediary active precursor of the enzyme, formed prior to dissociation into sub‐units. © 1999 Society of Chemical Industry
TI - Stability and stabilisation of penicillin acylase
JO - Journal of Chemical Technology & Biotechnology
DO - 10.1002/(SICI)1097-4660(199911)74:11<1110::AID-JCTB149>3.0.CO;2-B
DA - 1999-11-01
UR - https://www.deepdyve.com/lp/wiley/stability-and-stabilisation-of-penicillin-acylase-soxBGYEM4q
SP - 1110
EP - 1116
VL - 74
IS - 11
DP - DeepDyve
ER -