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dc.contributor.authorDevi, R-
dc.contributor.authorNampoothiri, KM-
dc.contributor.authorSukumaran, RK-
dc.contributor.authorSindhu, R-
dc.contributor.authorArumugam, M-
dc.identifier.citationJournal of Basic Microbiology;60(2):112-125en_US
dc.description.abstractA newly isolated culture, Pseudomonas guariconesis, is reported for the first time for lipase production. Various process parameters affecting enzyme production were optimized through statistical design experiments. The Plackett–Burman experimental design was used for screening 10 parameters for lipase production, which was further optimized using the central composite design of response surface methodology. Maximum lipase activity of 220 U/ml was obtained after 24 h of incubation in shake‐flask cultures with an inoculum concentration of 0.6% v/v, incubation temperature of 30°C, and medium pH 9.0. Castor oil (0.5% v/v) was used as the inducer for lipase production. The enzyme was found to be compatible with five different commercial detergents, indicating its potential to be used in detergent formulations. It also acted as a biocatalyst in a transesterification process. The alkaline enzyme was found to be stable in the presence of bleaching agents, metal ions, and organic solvents as well.en_US
dc.subjectcastor oilen_US
dc.subjectpseudomonas guariconesisen_US
dc.subjectresponse surface methodologyen_US
dc.subjectsubmerged fermentationen_US
dc.titleLipase of Pseudomonas Guariconesis as an Additive in Laundry Detergents and Transesterification Biocatalystsen_US
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