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

• Published in: Polish Journal of Chemical Technology
• Main Authors: Ulker, Cansu, Gokalp, Nurefsan, Guvenilir, Yuksel
• Format: Article in Journal/Newspaper
• Language: English
• Published: Walter de Gruyter GmbH 2016
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1515/pjct-2016-0060; http://content.sciendo.com/view/journals/pjct/18/3/article-p134.xml; https://www.sciendo.com/article/10.1515/pjct-2016-0060

Abstract 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.