Laccase‐catalyzed polymerization of lignocatechol and affinity on proteins of resulting polymers |
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Authors: | Takashi Yoshida Rong Lu Shuqin Han Kazuyuki Hattori Takahiro Katsuta Kei‐Ichi Takeda Kazutoshi Sugimoto Masamitsu Funaoka |
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Institution: | 1. Applied Chemistry Department, Kitami Institute of Technology, Koen‐Cho, Kitami 090‐8507, Japan;2. Department of Forest Products, Faculty of Bioresources, Mie University, Kamihama‐Cho, Tsu 514‐8507, Japan |
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Abstract: | For the synthesis of a new biologically functional polymer from a natural resource by an environment‐friendly method, the laccase‐catalyzed polymerization of a lignin‐based macromonomer, lignocatechol, was carried out for the first time in ethanol–phosphate buffer solvent system to give crosslinked polymers in good yields. Lignocatechol was prepared by the phase separation system of lignin and catechol in aqueous sulfuric acid. The copolymerization was also performed with urushiol to afford the corresponding copolymers in high yields. The polymerization mechanism was estimated by the IR and pyrolysis GC‐MS measurements, suggesting that the polymerization proceeded mainly at the catechol ring through a quinone radical intermediate. The thermal properties were measured by the DSC, TG, and TMA analyses, indicating that the polymers had high thermal stabilities because of the crosslinked structures. In addition, it was found that the resulting polymers had the affinity of bovine serum albumin (BSA) and glucoamylase. © 2008 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 47: 824–832, 2009 |
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Keywords: | affinity biological applications of polymers BSA enzymatic polymerization enzymes glucoamylase laccase lignophenols radical polymerization recycling thermal properties |
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