Wettability of pear leaves from three regions characterized at different stages after flowering using the OWRK method.

BACKGROUND: A better understanding of leaf surface wettability is critical to improve the adhesion of liquid pesticides. Leaf surface wettability is dependent on the property of the liquid as well as the physical and chemical properties of the leaf, which vary with climate and growth stage. The aim of this study was to characterize the wettability of pear leaves from three different climatic regions at different stages after flowering. RESULTS: The contact angles of different test liquids were measured on both adaxial and abaxial pear leaf surfaces and the Owens-Wendt-Rabel-Kaelble (OWRK) method was used to calculate surface free energy (SFE) and its polar and non-polar components. The results demonstrated that the SFE of both the adaxial and abaxial surface of the pear leaf, and the proportion of polar component, increased with increasing time after flowering. At early growth stages, pear leaves were highly hydrophobic, similar to a polytetrafluoroethylene surface, whereas at later growth stages, pear leaves were hydrophobic, more similar to a polymethylmethacrylate surface. Also, the SFE differed with climatic region. Factors influencing these changes are discussed. CONCLUSION: Changes in contact angles and SFE correlated with the change of the leaf surface wettability. Leaves became easier to wet (higher SFE), with an overall increasing polar component to the surface, with increasing age after flowering. As expected, changes in wettability were found in pear leaves at different stages after flowering and in different regions (P < 0.05). Pear leaves from Yuanping were easier to wet than leaves from Yuci and Linyi, and adaxial surfaces were easier to wet than abaxial surfaces. These results provide beneficial information for the application of agrochemicals for improved wetting and spreading behavior. © 2018 Society of Chemical Industry.

Equilibrium and dynamic interfacial properties of protein/ionic-liquid-type surfactant solutions at the decane/water interface.

The interfacial behavior of ß-casein and lysozyme solutions has been investigated in the presence of an ionic liquid-type imidazolium surfactant ([C16mim]Br) at the decane/water interface. The dynamic dilational properties of the protein/surfactant solutions are investigated by the oscillating drop method and interfacial tension relaxation method. The interfacial tension isotherms for the mixed adsorption layers indicate that the increased addition of [C16mim]Br to a pure protein changes the properties of the complex formed at the decane/water interface. Whereas the interfacial tension data of the protein/surfactant mixed layers do not clearly show differences with changing bulk composition, the dilational rheology provides undoubted evidence that the structure and, in particular, the dynamics of the adsorbed layers depend on the bulk surfactant concentration. The experiment data for ß-casein/[C16mim]Br solutions indicate that at higher bulk [C16mim]Br concentrations, ß-casein in the interfacial layer is subject to conformational changes, where it gives space to [C16mim]Br molecules in the form of coadsorb rather than replacement; in contrast, in lysozyme/[C16mim]Br solutions some lysozyme molecules desorb from the interface due to the competitive adsorption of free [C16mim]Br molecules. Experimental results related to the interfacial dilational properties of the protein/surfactant solutions show that the dilational modulus turns out to be more sensitive to the conformation of protein/surfactant mixture at the liquid interface than the interfacial tension.

Impact of ionic liquid-type imidazolium surfactant addition on dynamic properties of BSA adsorption layers at different pH.

The dynamic interfacial properties of mixed solutions of bovine serum albumin (BSA) and the ionic liquid-type imidazolium surfactant ([C16mim]Br) were measured as a function of the interface age, surfactant concentration and solution pH. Three BSA conformers were investigated: the normal N form as well as the fast F and aged A forms, corresponding to the different solution pH, respectively. The interfacial tension and the interfacial dilational elasticity isotherms for the mixed adsorption layers indicate that the addition of [C16mim]Br to the different structures of BSA isomers influences the properties of the adsorption layer at the decane/water interface. The addition of [C16mim]Br does not influence the structure of the protein at pH below the isoelectric point of BSA, but at higher solution pH, the addition of surfactants significantly influences the dynamic interfacial properties of BSA solutions due to the electrostatic interaction between the components.

Interaction of pepsin-[C16mim]Br system: interfacial dilational rheology and conformational studies.

The interfacial rheological property is closely related to the stabilities of foams and emulsions, yet there have been limited studies on the interaction between proteins with ionic liquid-type imidazolium surfactants at the decane-water interface as well as in the bulk. Herein, we investigated the interfacial and bulk properties of pepsin (PEP) and an ionic liquid (IL), 1-hexadecyl-3-methylimidazolium bromide, [C(16)mim]Br. The interfacial pressure and dilational rheology studies were performed to describe the formation of [C(16)mim]Br-pepsin complexes. The influence of the oscillating frequency and the bulk concentration of [C(16)mim]Br on the dilational properties were explored. The conformational changes were studied by monitoring the fluorescence and far UV-CD spectra. The results reveal that the globular structure of pepsin is one of the decisive factors controlling the nature of the interfacial film. The monotonous increase in the dilational elastic modulus of pepsin-[C(16)mim]Br solutions with the surface age indicates that no loops and tails had formed. Interestingly, with an increase in the concentration of [C(16)mim]Br, the εd-c curve first passes through a plateau value due to steric hindrance and the electrostatic barrier of already absorbed tenacious pepsin-[C(16)mim]Br complexes. With the further addition of [C(16)mim]Br, the remarkable decrease in dilational elastic modulus indicates that the compact structure is destroyed gradually. The results of the fluorescence spectra and far UV-CD spectra confirm that [C(16)mim]Br did not produce perceptible changes in pepsin at the concentrations studied in the dilational experiment. Possible schematic programs of the pepsin-[C(16)mim]Br interaction model at the interface and in bulk phase are proposed.

Research on the changes in wettability of rice (Oryza sativa.) leaf surfaces at different development stages using the OWRK method.

BACKGROUND: A good knowledge in wetting behavior of pesticide spray liquid on plant surface is crucial to spray applications. Difference in leaf surface wettability would result in obvious changes in spray wetting behavior. The aim of this paper is to obtain the changes of wettability during different growth periods. RESULTS: The contact angle (CA) of rice leaf for each liquid increased with rice growth. No significant difference was found between cultivars. The CA was found to be correlated with the polar component of liquid surface tension. The square of the polar component was also found to be highly significant indicating that the relationship between these two properties was not a simple linear one. The surface energy of each plant surface decreased as the plants aged. This was also true of each part of the surface energy. However, no obvious difference on the proportion of the components was found among different cultivars and stages. CONCLUSIONS: The changes in value of CA and surface free energy (SFE) both reflect the changes of the leaf surface wettability, while the SFE value shows better in wettability characterizing. Obvious rice leaf wettability changes were found on different development stages, which may be beneficial for researches in agrochemical sprays wetting and spreading behavior. Factors influencing these alterations were discussed.

[Study on determination of acetamiprid and interaction between acetamiprid and deoxyribonucleic acid by resonance light scattering].

The interaction between acetamiprid and deoxyribonucleic acid (DNA) was used to determine acetamiprid by resonance light scattering (RLS). The RLS signals of DNA were greatly enhanced by acetamiprid in the spectrum region of 300-600 nm. The spectrum peak is around 316.0 nm. The optimum conditions: pH is 1.73; the concentration of DNA is 2.0 microg x mL(-1)bration curve is 0-2. 25 pg * mLU , with the detection2limit of 0. 2 ig * mL '. The acetamiprid in river water sample was determined. The results were satisfactory, and the recovery rates were in the range of 98%-106%. The interaction mechanism of acetamiprid and DNA was discussed: the interactions between acetamiprid and nucleic acid base include electrostatic effect and Tr-r cumulate effect.