Simultaneous production of exopolysaccharide and lipase from extremophylic Pseudomonas aeruginosa san-ai strain: A novel approach for lipase immobilization and purification

In this study, exopolysaccharide (EPS) produced by an extremophylic strain of Pseudomonas aeruginosa san-ai was used as a support for immobilization of lipase produced together with EPS, using new and simple, single step procedure. The highest EPS production (36.5 mg L −1) was observed in the Luria...

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Bibliographic Details
Published in:Carbohydrate polymers 2011-01, Vol.83 (3), p.1397-1401
Main Authors: Dimitrijević, Aleksandra, Veličković, Dušan, Rikalović, Milena, Avramović, Nataša, Milosavic, Nenad, Jankov, Ratko, Karadžić, Ivanka
Format: Article
Language:English
Subjects:
Applied sciences
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
calcium chloride
Entrapment
Exact sciences and technology
Exopolysaccharide
exopolysaccharides
Fourier transform infrared spectroscopy
Fundamental and applied biological sciences. Psychology
Immobilization of enzymes and other molecules
Immobilization techniques
immobilized enzymes
Lipase
Methods. Procedures. Technologies
Natural polymers
nuclear magnetic resonance spectroscopy
Physicochemistry of polymers
polysorbates
Pseudomonas aeruginosa
Pseudomonas aeruginosa san-ai
Starch and polysaccharides
sunflower oil
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Summary:In this study, exopolysaccharide (EPS) produced by an extremophylic strain of Pseudomonas aeruginosa san-ai was used as a support for immobilization of lipase produced together with EPS, using new and simple, single step procedure. The highest EPS production (36.5 mg L −1) was observed in the Luria Bertani (LB) medium supplemented with sunflower oil and Tween 80. The EPS structure was analyzed by FT-IR and 1H NMR, and it was found that EPS from P. aeruginosa is of the alginate type. Lipase, produced by the same strain was entrapped in Ca–EPS beads, formed by dripping a concentrated culture supernatant in CaCl 2 solutions. Effects of immobilization conditions on loading efficiency and immobilization yield were investigated, and the potential for reuse of immobilized lipase was monitored. It was shown that the immobilized enzyme could be used for up to three reaction cycles, after which 77% of activity was retained.
ISSN:0144-8617
1879-1344
DOI:10.1016/j.carbpol.2010.10.005