P. Helisto et T. Korpela, EFFECTS OF DETERGENTS ON ACTIVITY OF MICROBIAL LIPASES AS MEASURED BYTHE NITROPHENYL ALKANOATE ESTERS METHOD, Enzyme and microbial technology, 23(1-2), 1998, pp. 113-117
Enzymatic activities of lipases from Chromobacterium viscosum, Pseudom
onas fluorescens, Bacillus sp., Candida cylindracea, Aspergillus carne
us, and Penicillium sp. were compared with the spectrophotometric p-ni
trophenylbutyrate (pNB) assay at different concentrations of the deter
gents Tween 20, Triton X-100, polyvinyl alcohol (LALLS), and linear al
kylbenzene sulfonate (LAS). The activities of lipases from C. cylindra
cea and C. viscosum were additionally measured with sodium desoxychola
te (bile salt BL), hexadecyl trimethyl ammonium bromide (CTAB), and Tw
een 80. The maximal activities of eukaryotic lipases were generally at
the lower concentrations of detergents than those of prokaryotic lipa
ses. All detergents, including the anionic detergent BL, inhibited euk
aryotic lipases very effectively. LAS and CTAB stimulated C. viscosum
lipase above their critical micellar concentrations (CMC), but CTAB di
d not increase the activity of C. cylindracea lipase at all, although
even a low concentration of LAS inhibited its activity. The other euka
ryotic lipases behaved with LAS similarly to C. cylindracea lipase. It
is more tedious to find proper detergent for eucaryotic than prokaryo
tic lipase, because the detergents seem to stimulate eukaryotic lipase
s in a very narrow range or low concentrations. Prolonged incubation w
ith LAS decreased the activity of eukaryotic lipases effectively but p
rokaryotic lipases only little. LALLS could be a good detergent for th
e prokaryotic lipase reactions because it inhibited activity only a li
ttle. The most significant observation was the high detergent toleranc
e of Bacillus sp. lipase, it can be concluded that eukaryotic and prok
aryotic lipases roughly Sor-m two separate classes behaving guile diff
erently in different detergents. (C) 1998 Elsevier Science Inc.