ANALYTICA CHIMICA ACTA
·
2024
·
IF 5.7
Yingying Zhong,Qing Wang,Zi-Jian Chen,Hongwu Wang,Suqing Zhao
Background In vitro screening strategies based on the inhibition of α-glucosidase (GAA) activity have been widely used for the discovery of potential antidiabetic drugs, but they still face some challenges, such as poor enzyme stability, non-reusability and narrow range of applicability. To overcome these limitations, an in vitro screening method based on GAA@GOx@Cu-MOF reactor was developed in our previous study. However, the method was still not satisfactory enough in terms of construction cost, pH stability, organic solvent resistance and reusability. Thence, there is still a great need for the development of in vitro screening methods with lower cost and wider applicability. Results A colorimetric sensing strategy based on GAA/(Au–Au/IrO 2 )@Cu(PABA) cascade catalytic reactor, which constructed through simultaneous encapsulating Au–Au/IrO 2 nanozyme with glucose oxidase-mimicking and peroxidase-mimicking activities and GAA in Cu(PABA) carrier with peroxidase-mimicking activity, was innovatively developed for in vitro screening of GAA inhibitors in this work. It was found that the reactor not only exhibited excellent thermal stability, pH stability, organic solvent resistance, room temperature storage stability, and reusability, but also possessed cascade catalytic performance, with approximately 12.36-fold increased catalytic activity compared to the free system (GAA + Au–Au/IrO 2 ). Moreover, the in vitro GAA inhibitors screening method based on this reactor demonstrated considerable anti-interference performance and detection sensitivity, with a detection limit of 4.79 nM for acarbose. Meanwhile, the method owned good reliability and accuracy, and has been successfully applied to the in vitro screening of oleanolic acid derivatives as potential GAA inhibitors. Significance This method not only more effectively solved the shortcomings of poor stability, narrow scope of application, and non-reusability of natural enzymes in the classical method compared with our previous work, but also broaden the application scope of Au–Au/IrO 2 nanozyme with glucose oxidase and peroxidase mimicking activities, and Cu(PABA) carrier with peroxidase mimicking activity, which was expected to be a new generation candidate method for GAA inhibitor screening.
研究领域:
生物技术
·
催化
·
药物发现
·
酶学
·
分析化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
ACS Applied Materials & Interfaces
·
2021
·
IF 9.229
Yingying Zhong,Tiantian Wang,Zhiting Lao,Minglei Lu,Shan Liang,Xiping Cui,Qing-lan Li,Suqing Zhao
Herein, a Au-Au/IrO2 nanocomposite with tandem enzyme-mimicking activity was innovatively synthesized, which can show outstanding glucose oxidase (GOx)-like activity and peroxidase-like activity simultaneously under neutral conditions. Moreover, a Au-Au/IrO2@Cu(PABA) reactor was prepared via encapsulation of the Au-Au/IrO2 nanocomposite in a Cu(PABA) metal organic framework. The reactor not only exhibits excellent organic solvent stability, acid resistance, and reusability but also displays better cascade reaction catalytic efficiency (kcat/Km = 148.86 min–1 mM–1) than the natural free enzyme system (GOx/HRP) (kcat/Km = 98.20 min–1 mM–1) and Au-Au/IrO2 nanocomposite (kcat/Km = 135.24 min–1 mM–1). In addition, it is found that the reactor can catalyze glucose or dissolved oxygen to produce active oxygen species (ROS) including HO, 1O2, and O2–· through its enzyme-mimicking activity. Finally, the novel reactor was successfully used in organic dye degradation and antibacterial application. The results show that it can effectively degrade methyl orange, methylene blue, and rhodamine B, which all can reach a degradation rate of nearly 100% after interacting with Au-Au/IrO2@Cu (PABA) for 3.5 h. Furthermore, the reactor also exhibits excellent antibacterial activity, so as to achieve a complete bactericidal effect to Staphylococcus aureus and Escherichia coli at a concentration of 12.5 μg mL–1.
研究领域:
纳米材料
·
催化
·
环境科学
·
材料科学
·
生物技术
✓ 已验证
DOI
PubMed
高影响因子
PROCESS BIOCHEMISTRY
·
2024
·
IF 3.7
Hongbo Suo,Xinzheng Liu,Shu Chen,Qi Li,Xiangnan Liu,Lili Xu
Biodiesel is more environmentally friendly compared to traditional petroleum diesel. The method of producing biodiesel catalyzed by lipases, as a green chemistry technology, can further reduce its negative impact on the environment. In this work, lipase immobilized on magnetic cellulose was embedded in Cu(PABA), and then the biocomposite (MCL@Cu(PABA)) was used for biodiesel production. The good biocompatibility and flexible skeleton structure of cellulose can buffer the compression effect on enzyme molecules during the formation of Metal-Organic Frameworks (MOFs), and the MOFs protective layer can reduce the damage caused by denaturants to enzyme molecules. The biocatalyst showed enhanced activity and stability with a lower deactivation constant ( K d ). Under the optimized reaction conditions, the biodiesel yield can reach 78.4 %. After reused for 7 times, the biocatalyst can still achieve a biodiesel yield of 58.8 %. Moreover, after stored for 30 days, the biodiesel yield can still reach 70.3 %. For all experimental yields, the standard deviation (SD) ranged from 2.4 % to 4.5 %. Secondary structure analysis showed that the rigid structure and active conformation of lipase was enhanced after Cu(PABA) encapsulation.
研究领域:
生物化学
·
环境科学
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）