TY - JOUR ID - 14805 TI - Enzymatic Ring Opening Polymerization Of É›-caprolactone By Using A Novel Immobilized Biocatalyst JO - Advanced Materials Letters JA - AML LA - en SN - 0976-3961 AU - Gokalp, Nurefsan AU - Ulker, Cansu AU - Avcibasi Guvenilir, Yuksel AD - Y1 - 2016 PY - 2016 VL - 7 IS - 2 SP - 144 EP - 149 KW - Candida antarctica lipase B KW - ring opening polymerization KW - É KW - &rsaquo KW - CL KW - immobilization KW - crosslinking DO - 10.5185/amlett.2016.6059 N2 - In this study, an amorphous silica material was used as a carrier to immobilize Candida antarctica lipase B (CALB) by crosslinking method for ring opening polymerization of É›-caprolactone (É›-CL). The optimum temperature, enzyme concentration and time period were investigated for poly(É›-caprolactone) (PCL) synthesis via ring opening polymerization of É›-CL catalyzed by immobilized CALB (IMCALB). Molecular weights of PCLs were determined by using gel permeation chromatography (GPC) and hydrogen nuclear magnetic resonance ( 1 H-NMR) analysis. The surface morphologies of PCLs were analyzed by scanning electron microscopy (SEM). Besides, PCLs were successfully characterized by fourier transform infrared spectroscopy (FTIR), thermal gravimetric analysis (TGA) and differential scanning calorimetry (DSC) analysis. The results showed that the immobilized lipase by crosslinking method via glutaraldehyde possessed good activity and stability. By using this immobilized enzyme, high molecular weights and monomer conversions of PCLs were achieved about 9000 g/mol and     90 %, respectively. This work has showed that activity of CALB increased about 17 % dramatically after immobilization process, and PCL was synthesized via enzymatic polymerization catalyzed this novel enzyme, which provides an effective method for conducting “green polymer chemistry”.  UR - https://aml.iaamonline.org/article_14805.html L1 - https://aml.iaamonline.org/article_14805_6c30c65c67d6ffcf2835fdf05beafd9f.pdf ER -