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1.
ACS Omega ; 4(26): 22057-22068, 2019 Dec 24.
Artigo em Inglês | MEDLINE | ID: mdl-31891086

RESUMO

Herein, we present a greener approach to achieve an ultrasensitive, selective, and viable sensor engineered by amino acids as a recognition layer for simultaneous electrochemical sensing of toxic heavy metals (HMs). Electrochemical techniques like electrochemical impedance spectroscopy (EIS), cyclic voltammetry (CV), and square-wave anodic stripping voltammetry (SWASV) were applied to demonstrate sensing capabilities of the designed analytical tool. The comparative results of different amino acids demonstrate alanine's superior performance with a well-resolved and enhanced current signal for target metal ions due to strong complexation of its functional moieties. The working conditions for alanine-modified GCE were optimized by investigating the effect of alanine concentration, different supporting electrolytes, pH values, accumulation potentials, and time. The limits of detection for Zn2+, Cd2+, Cu2+, and Hg2+ were found to be 8.92, 5.77, 3.01, and 5.89 pM, respectively. The alanine-modified electrode revealed absolute discrimination ability, stability, and ultrasensitivity toward metal ions even in the presence of multifold interfering species. Likewise, greener modifier-designed electrodes possessed remarkable electrocatalytic activity, cost affordability, reproducibility, and applicability for picomolar level detection of HM ions in real water sample matrixes. Theoretical calculations for the HM-amino acid interaction also support a significantly improved mediator role of the alanine modifier that is consistent with the experimental findings.

2.
J Dairy Res ; 85(4): 460-464, 2018 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-30136638

RESUMO

Lactoperoxidase (LPO) is an antimicrobial protein present in milk that plays an important role in natural defence mechanisms during neonatal and adult life. The antimicrobial activity of LPO has been commercially adapted for increasing the shelf life of dairy products. Immobilization of LPO on silver nanoparticles (AgNPs) is a promising way to enhance the antimicrobial activity of LPO. In the current study, LPO was immobilized on AgNPs to form LPO/AgNP conjugate. The immobilized LPO/AgNP conjugate was characterized by various biophysical techniques. The enhanced antibacterial activity of the conjugate was tested against E. coli in culture at 2 h intervals for 10 h. The results showed successful synthesis of spherical AgNPs. LPO was immobilized on AgNPs with agglomerate sizes averaging approximately 50 nm. The immobilized conjugate exhibited stronger antibacterial activity against E. coli in comparison to free LPO. This study may help in increasing the efficiency of lactoperoxidase system and will assist in identifying novel avenues to enhance the stability and antimicrobial function of LPO system in dairy and other industries.


Assuntos
Enzimas Imobilizadas/farmacologia , Escherichia coli/efeitos dos fármacos , Lactoperoxidase/farmacologia , Nanopartículas Metálicas/química , Prata/química , Antibacterianos/química , Antibacterianos/farmacologia , Enzimas Imobilizadas/química , Enzimas Imobilizadas/metabolismo , Lactoperoxidase/química , Lactoperoxidase/metabolismo
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