Lipase biocatalytic processes in surfactant free microemulsion-like ternary systems and related organogels

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Lipase biocatalytic processes in surfactant free microemulsion-like ternary systems and related organogels

Ζουμπανιώτη, Μαρία
Ξενάκης, Αριστοτέλης
Karali, M.
Stamatis, H.

Άρθρο σε επιστημονικό περιοδικό

2006


Lipases from Rhizomucor miehei (RmL) and Candida antartcica (CaL-B) entrapped in surfactant free microemulsion-like ternary systems consisting of n-hexane, short chain alcohols (1-propanol or 2-methyl-2-propanol) and water, keep their catalytic activity at 30 ◦C, catalyzing efficiently the esterification of fatty acids or natural phenolic acids including cinnamic acid derivatives. High conversions (up to 95%) were obtained with both lipases entrapped in various ternary systems. Lipases catalytic efficiency and stability was influenced by the composition of the ternary systems used. Hydroxypropylmethyl cellulose (HPMC) microemulsions-based organogels (MBGs) formulated with various surfactant free microemulsion-like systems were used as a matrix for enzyme immobilization. These lipase-containing MBGs prove to be a novel solid-phase catalyst for use, under mild conditions, in non-polar solvents as well as in solvent free systems. CaL-B immobilized in surfactant free MBGs keep its catalytic activity for a storage period of 8 months, while the corresponding residual activity of immobilized RmL was decreased by 50%. The stability of enzymes in such surfactant free MBGs is higher than that observed in MBGs formulated with surfactant based w/o microemulsions. Lipases-containing surfactant free MBGs were used in seven consecutive batch syntheses of fatty esters with only 10–15% loss of activity.

Βιολογία (Γενικά) (EL)
Βιοτεχνολογία (EL)
Επιστήμη (EL)
Biology (General) (EN)
Biotechnology (EN)
Science (EN)

Surfactant free microemulsions
Stability
Immobilization
Organogels
Lipase
Esterification
Phenolic acids

English

Elsevier Inc.


Enzyme and Microbial Technology

https://creativecommons.org/licenses/by/4.0/deed.el
Copyright @ Elsevier
Copyright @ Elsevier (EN)




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