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Activity and stability of Penicillium cyclopium lipase in surfactant and detergent solutions
Author(s) -
Xia J.,
Chen X.,
Nnanna I. A.
Publication year - 1996
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02523457
Subject(s) - lipase , chemistry , pulmonary surfactant , sodium dodecyl sulfate , sulfonate , alkyl , sodium , triacylglycerol lipase , ethanol , chromatography , organic chemistry , enzyme , biochemistry
Activity and stability of an alkaline lipase from Penicillium cyclopium var. album (PG 37) were studied in surfactant and detergent solutions. Three anionic surfactants [Na salts of C 12 SO 4 − (sodium dodecyl sulfate), C 12 ØSO 3 / − (linear alkyl benzene sulfonate), and C 11 COO − (laurate)] and four homologous series of nonionic surfactants of C 12–15 polyoxethylenated fatty alcohols (AEO 3 , AEO 5 , AEO 7 , and AEO 9 ) were evaluated. At a concentration range of 3.2–40 μM, sodium dodecyl sulfate and laurate stimulated the activity of PG 37 lipase. At concentrations greater than 5.6 μM, linear alkylbenzene sulfonate inhibited PG 37 lipase activity. Nonionic surfactants, AEO 5 and AEO 7 , in the concentration range of 0.25–20 mM, enhanced and stabilized the activity of PG 37 lipase. The presence of PG 37 lipase in detergent formulaton improved detergency ∼20%. The mechanism of inhibition of the lipolytic activity of PG 37 lipase is proposed to be partly due to the formation of inactive (BR) n ‐E complex between the hydrophobic moiety of the surfactants and the surface of the lipase. Conversely, formation of a soluble (RB) n ‐E complex between the hydrophilic group of the surfactant and lipase may account for the increased lipolytic activity of PG 37 lipase.