Lipases and proteases produced by indigenous Pseudomonas aeruginosa strain as potential detergent additives

Enzymes produced by indigenous Pseudomonas aeruginosa strain have been subjected to research considering their potential application as detergent additives. As previously noted, lipase produced by Pseudomonas aeruginosa is highly alkaline, thermostable and solvent tolerant. Furthermore, same strain...

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Published inHemijska industrija Vol. 63; no. 4; pp. 331 - 335
Main Authors Grbavčić, S.Ž., Tehnološko-metalurški fakultet, Beograd (Serbia), Bezbradica, D.I., Tehnološko-metalurški fakultet, Beograd (Serbia), Karadžić, I.M., Medicinski fakultet, Beograd (Serbia), Knežević-Jugović, Z.D., Tehnološko-metalurški fakultet, Beograd (Serbia)
Format Journal Article
LanguageEnglish
Published Association of Chemical Engineers of Serbia 2009
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Summary:Enzymes produced by indigenous Pseudomonas aeruginosa strain have been subjected to research considering their potential application as detergent additives. As previously noted, lipase produced by Pseudomonas aeruginosa is highly alkaline, thermostable and solvent tolerant. Furthermore, same strain exhibits both lipase and protease activity establishing this lipase as potentially desirable component of enzyme-containing detergents. Further research was carried out to investigate insusceptibility of this lipase against coexisting native protease, several commercial surfactants, oxidizing agents and commercial detergents. Lipases and proteases remained highly active when incubated with several different surfactants and oxidizing agents under washing conditions. Moreover, presence of surfactants and oxidizing agents such as Tween(R) 20 and Triton(R) X-100 initially augment lipase and protease activity. Additionally, crude lipase preparation was insusceptible to coexisting native protease hence indicating possible storage stability. Overall, the remarkable properties of these enzymes make them potential detergent additives.
Bibliography:COBISS.SR-ID 44055
Q02
ISSN:0367-598X
2217-7426
DOI:10.2298/HEMIND0904331G