GÖktÜrk Ersen
Department of Chemistry, Faculty of Arts and Science, Hatay Mustafa Kemal University, Hatay Turkey.
Turk J Chem. 2020 Oct 26;44(5):1285-1292. doi: 10.3906/kim-2005-32. eCollection 2020.
In this study, the catalytic activity and stability of flowerlike hybrid horseradish peroxidase (HRP) nanobiocatalyst (HRP-Cu ) obtained from Cu ions and HRP enzyme in the polymerization reaction of guaiacol were analyzed. We demonstrated that HRP-Cu and hydrogen peroxide (H O ) initiator showed significantly increased catalytic activity and stability on the polymerization of guaiacol compared to that of free HRP enzyme. Poly(guaiacol) was observed with quite high yields (88%) and molecular weights (38,000 g/mol) under pH 7.4 phosphate-buffered saline (PBS) conditions at 60 °C with 5 weight% of HRP-Cu loading. HRP-Cu also shows very high thermal stability and works even at 70 °C reaction temperature; free HRP enzyme denatures at that temperature. Furthermore, HRP-Cu provided considerable repeated use and showed some degree of catalytic activity, even after the fourth recycle, in the polymerization of guaiacol.
在本研究中，分析了由铜离子和辣根过氧化物酶（HRP）在愈创木酚聚合反应中获得的花状杂化辣根过氧化物酶（HRP-Cu ）纳米生物催化剂的催化活性和稳定性。我们证明，与游离HRP酶相比，HRP-Cu 和过氧化氢（H O ）引发剂在愈创木酚聚合反应中表现出显著提高的催化活性和稳定性。在60°C、pH 7.4的磷酸盐缓冲盐水（PBS）条件下，当HRP-Cu 负载量为5 wt%时，观察到聚愈创木酚的产率相当高（88%），分子量为38,000 g/mol。HRP-Cu 还表现出非常高的热稳定性，甚至在70°C的反应温度下也能起作用；游离HRP酶在该温度下会变性。此外，HRP-Cu 具有相当高的重复使用性，即使在第四次循环后，在愈创木酚聚合反应中仍表现出一定程度的催化活性。
