Polypyrrole/silica/magnetite nanoparticles as a sorbent for the extraction of sulfonamides from water samples

A magnetic solid‐phase extraction sorbent of polypyrrole/silica/magnetite nanoparticles was successfully synthesized and applied for the extraction and preconcentration of sulfonamides in water samples. The magnetite nanoparticles provided a simple and fast separation method for the analytes in water samples. The silica coating increased the surface area that helped to increase the polypyrrole layer. The polypyrrole‐coated silica provided a high extraction efficiency due to the π–π and hydrophobic interactions between the polypyrrole and sulfonamides. Several parameters that affected the extraction efficiencies, i.e. the amount of sorbent, pH of the sample, extraction time, extraction temperature, ionic strength, and desorption conditions were investigated. Under the optimal conditions, the method was linear over the range of 0.30–200 μg/L for sulfadiazine and sulfamerazine, and 1.0–200 μg/L for sulfamethazine and sulfamonomethoxine. The limit of detection was 0.30 μg/L for sulfadiazine and sulfamerazine and 1.0 μg/L for sulfamethazine and sulfamonomethoxine. This simple and rapid method was successfully applied to efficiently extract sulfonamides from water samples. It showed a high extraction efficiency for all tested sulfonamides, and the recoveries were in the range of 86.7–99.7% with relative standard deviations of < 6%.     

Current knowledge on the extraction,purification, identification,and validation of bioactive peptides from seaweed

Seaweed (macroalgae) is considered as a sustainable bioresource rich in high-quality nutrients such as protein. Seaweed protein can be used as an alternative to other protein sources. Furthermore, these proteins are natural reservoirs of bioactive peptides (BAPs) associated with various health benefits such as antioxidant, antihypertensive, and antidiabetic activities. However, seaweed-derived BAPs remain underexploited due to challenges that arise during protein extraction from algal biomass. Coupled with this, limited proteomic information exists regarding certain seaweed species. This review highlights the current state of the art of seaweed protein extraction techniques, e.g., liquid, ultrasound, microwave, pulsed electric field, and high hydrostatic pressure assisted extraction. The review also focuses on the enzymatic hydrolysis of seaweed proteins and characterization of the resultant hydrolysates/peptides using electrophoretic and chromatographic techniques. This includes reference to methods employed for separation, fractionation, and purification of seaweed BAPs, as well as the methodologies used for identification, e.g., analysis by mass spectrometry. Furthermore, a bioinformatics or in silico approach to aid discovery of seaweed BAPs is discussed herein. Based on the information available to date, it is suggested that further research is required in this area for the development of seaweed BAPs for nutraceutical applications.     

One‐Pot Bioconversion of l‐Arabinose to l‐Ribulose in an Enzymatic Cascade

This work reports the one‐pot enzymatic cascade that completely converts l ‐arabinose to l ‐ribulose using four reactions catalyzed by pyranose 2‐oxidase (P2O), xylose reductase, formate dehydrogenase, and catalase. As wild‐type P2O is specific for the oxidation of six‐carbon sugars, a pool of P2O variants was generated based on rational design to change the specificity of the enzyme towards the oxidation of l ‐arabinose at the C2‐position. The variant T169G was identified as the best candidate, and this had an approximately 40‐fold higher rate constant for the flavin reduction (sugar oxidation) step, as compared to the wild‐type enzyme. Computational calculations using quantum mechanics/molecular mechanics (QM/MM) molecular dynamics (MD) showed that this improvement is due to a decrease in the steric effects at the axial C4‐OH of l ‐arabinose, which allows a reduction in the distance between the C2‐H and flavin N5, facilitating hydride transfer and enabling flavin reduction.     

Fabrication of a chitin/chitosan hydrocolloid wound dressing and evaluation of its bioactive properties

Research on Chemical Intermediates - The aim of this study was to develop a chitin/chitosan hydrocolloid (CCH) wound dressing. Chitosan was cross-linked with tripolyphosphate to prepare chitosan...     

The Mechanism of Sugar C−H Bond Oxidation by a Flavoprotein Oxidase Occurs by a Hydride Transfer Before Proton Abstraction

Understanding the reaction mechanism underlying the functionalization of C−H bonds by an enzymatic process is one of the most challenging issues in catalysis. Here, combined approaches using density functional theory (DFT) analysis and transient kinetics were employed to investigate the reaction mechanism of C−H bond oxidation in d -glucose, catalyzed by the enzyme pyranose 2-oxidase (P2O). Unlike the mechanisms that have been conventionally proposed, our findings show that the first step of the C−H bond oxidation reaction is a hydride transfer from the C2 position of d -glucose to N5 of the flavin to generate a protonated ketone sugar intermediate. The proton is then transferred from the protonated ketone intermediate to a conserved residue, His548. The results show for the first time how specific interactions around the sugar binding site promote the hydride transfer and formation of the protonated ketone intermediate. The DFT results are also consistent with experimental results including the enthalpy of activation obtained from Eyring plots, as well as the results of kinetic isotope effect and site-directed mutagenesis studies. The mechanistic model obtained from this work may also be relevant to other reactions of various flavoenzyme oxidases that are generally used as biocatalysts in biotechnology applications.