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脲酶杂交纳米花的合成及其增强的催化性能。

Synthesis of urease hybrid nanoflowers and their enhanced catalytic properties.

作者信息

Somturk Burcu, Yilmaz Ismail, Altinkaynak Cevahir, Karatepe Aslıhan, Özdemir Nalan, Ocsoy Ismail

机构信息

Department of Chemistry, Faculty of Science, Erciyes University, Kayseri 38039, Turkey.

Department of Analytical Chemistry, Faculty of Pharmacy, Erciyes University, 38039 Kayseri, Turkey; Nanotechnology Research Center, Erciyes University, Kayseri 38039, Turkey.

出版信息

Enzyme Microb Technol. 2016 May;86:134-42. doi: 10.1016/j.enzmictec.2015.09.005. Epub 2015 Sep 14.

Abstract

Increasing numbers of materials have been extensively used as platforms for enzyme immobilization to enhance catalytic activity and stability. Although stability of enzyme was accomplished with immobilization approaches, activity of the most of the enzymes was declined after immobilization. Herein, we synthesize the flower shaped-hybrid nanomaterials called hybrid nanoflower (HNF) consisting of urease enzyme and copper ions (Cu(2+)) and report a mechanistic elucidation of enhancement in both activity and stability of the HNF. We demonstrated how experimental factors influence morphology of the HNF. We proved that the HNF (synthesized from 0.02mgmL(-1) urease in 10mM PBS (pH 7.4) at +4°C) exhibited the highest catalytic activity of ∼2000% and ∼4000% when stored at +4°C and RT, respectively compared to free urease. The highest stability was also achieved by this HNF by maintaining 96.3% and 90.28% of its initial activity within storage of 30 days at +4°C and RT, respectively. This dramatically enhanced activity is attributed to high surface area, nanoscale-entrapped urease and favorable urease conformation of the HNF. The exceptional catalytic activity and stability properties of HNF can be taken advantage of to use it in fields of biomedicine and chemistry.

摘要

越来越多的材料被广泛用作酶固定化的平台,以提高催化活性和稳定性。尽管通过固定化方法实现了酶的稳定性,但大多数酶在固定化后活性下降。在此,我们合成了由脲酶和铜离子(Cu(2+))组成的花状杂化纳米材料,即杂化纳米花(HNF),并报告了HNF活性和稳定性增强的机理阐释。我们展示了实验因素如何影响HNF的形态。我们证明,与游离脲酶相比,(在4°C下由10mM PBS(pH 7.4)中0.02mgmL(-1)脲酶合成的)HNF在4°C和室温下储存时分别表现出约2000%和约4000%的最高催化活性。通过在4°C和室温下分别储存30天内保持其初始活性的96.3%和90.28%,该HNF也实现了最高稳定性。这种显著增强的活性归因于HNF的高表面积、纳米级包裹的脲酶和有利的脲酶构象。HNF卓越的催化活性和稳定性特性可被利用于生物医学和化学领域。

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