Enzymatic synthesis and characterization of polycaprolactone by using immobilized lipase onto a surface-modified renewable carrier

In the present study, rice husk ash, which is a renewable and abundant material, was utilized as a carrier for lipase immobilization for the first time. Poly (ε-caprolactone) synthesis was successfully achieved by the new enzymatic catalyst: Candida antarctica lipase B immobilized onto surface-modif...

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Bibliographic Details
Published in:Polish Journal of Chemical Technology
Main Authors: Ulker Cansu, Gokalp Nurefsan, Guvenilir Yuksel
Format: Article in Journal/Newspaper
Language:English
Published: Sciendo 2016
Subjects:
Online Access:https://doi.org/10.1515/pjct-2016-0060
https://doaj.org/article/6d4a2baeae964663b39bca037999d66c
Description
Summary:In the present study, rice husk ash, which is a renewable and abundant material, was utilized as a carrier for lipase immobilization for the first time. Poly (ε-caprolactone) synthesis was successfully achieved by the new enzymatic catalyst: Candida antarctica lipase B immobilized onto surface-modified rice husk ashes by covalent binding. It was aimed to obtain optimum polymerization conditions at which highest molecular weight was reached and characterize the polymer produced. Moreover, thermal stability and effectiveness of the new biocatalyst in non-aqueous media were also shown with successful polymerization reactions. In addition, by using the new enzyme preparation, ε-caprolactone was able to be polymerized even at 30°C, which was promising for an energy saving process. Consequently, this work provides a new alternative route for poly (ε-caprolactone) synthesis.