Magro Massimiliano, Baratella Davide, Venerando Andrea, Nalotto Giulia, Basso Caroline R, Molinari Simone, Salviulo Gabriella, Ugolotti Juri, Pedrosa Valber A, Vianello Fabio
Department of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell'Università 16, 35020 Legnaro (PD), Italy.
Department of Chemistry and Biochemistry, Institute of Bioscience, Universidade Estadual Paulista, Botucatu, SP 18618-000, Brazil.
Materials (Basel). 2020 Apr 10;13(7):1776. doi: 10.3390/ma13071776.
Generally, enzyme immobilization on nanoparticles leads to nano-conjugates presenting partially preserved, or even absent, biological properties. Notwithstanding, recent research demonstrated that the coupling to nanomaterials can improve the activity of immobilized enzymes. Herein, xanthine oxidase (XO) was immobilized by self-assembly on peculiar naked iron oxide nanoparticles (surface active maghemite nanoparticles, SAMNs). The catalytic activity of the nanostructured conjugate (SAMN@XO) was assessed by optical spectroscopy and compared to the parent enzyme. SAMN@XO revealed improved catalytic features with respect to the parent enzyme and was applied for the electrochemical studies of xanthine. The present example supports the nascent knowledge concerning protein conjugation to nanoparticle as a means for the modulation of biological activity.
一般来说，酶固定在纳米颗粒上会导致纳米缀合物呈现出部分保留甚至缺失的生物学特性。尽管如此，最近的研究表明，与纳米材料偶联可以提高固定化酶的活性。在此，黄嘌呤氧化酶（XO）通过自组装固定在特殊的裸氧化铁纳米颗粒（表面活性磁赤铁矿纳米颗粒，SAMNs）上。通过光谱法评估了纳米结构缀合物（SAMN@XO）的催化活性，并与亲本酶进行了比较。与亲本酶相比，SAMN@XO显示出更好的催化特性，并被用于黄嘌呤的电化学研究。本实例支持了有关蛋白质与纳米颗粒缀合作为调节生物活性手段的新认识。
