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Lipase of Pseudomonas guariconesis as an additive in laundry detergents and transesterification biocatalysts
Author(s) -
Devi Rajan,
Madhavan Nampoothiri Kesavan,
Sukumaran Rajeev Kumar,
Sindhu Raveendran,
Arumugam Muthu
Publication year - 2020
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201900326
Subject(s) - lipase , transesterification , chemistry , castor oil , central composite design , response surface methodology , biocatalysis , plackett–burman design , chromatography , pseudomonas , fractional factorial design , factorial experiment , organic chemistry , enzyme , methanol , catalysis , biology , bacteria , ionic liquid , statistics , mathematics , genetics
A 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.