The tribological properties of zinc borate ultrafine powder as a lubricant additive in sunflower oil

This paper presents an investigation on the tribological properties of zinc borate ultrafine powder employed as a lubricant additive in sunflower oil. The stable dispersions of 0.5 wt%, 1 wt% and 2 wt% zinc borate ultrafine powder in sunflower oil were achieved by using an ultrasonic homogeniser. Both a 4-ball tester and a pin-on-disc tester were employed to evaluate the anti-wear and friction reduction capabilities of zinc borate ultrafine powder. Tribo-films with dark colour were generated on the worn surfaces and showed a good contrast with the substrate. The worn surface with different morphologies reflected as the colour alterations on the worn surface were observed when different lubricants were applied. The morphology and elemental analysis of the worn surfaces were studied using atomic force microscopy (AFM) and scanning electronic microscopy (SEM). Mechanical properties of the tribo-films and substrates were studied with a nano-indentation tester. Test results suggest that tribo-films generated on the worn surface have a relatively low hardness compared with the steel substrate. The substrates on the worn surfaces lubricated in sunflower oil with the powder demonstrated higher hardness than that of the substrate lubricated with pure sunflower oil due to the possible tribo-chemical reaction between the zinc borate additive and substrate. The combination of sunflower oil with 0.5% zinc borate ultrafine powder has delivered the most balanced performance in friction and wear reduction. This study has demonstrated the possibility of application of this industrially applicable solid lubricant additive (zinc borate) with a decomposable vegetable based lubricant oil.Peer reviewedFinal Accepted Versio

Evidence for Two Gaps and Breakdown of the Uemura Plot in Ba0.6_{0.6}K0.4_{0.4}Fe2_2As2_2 Single Crystals

We report a detailed investigation on the lower critical field $H_{c1}$ of the superconducting Ba$_{0.6}$K$_{0.4}$Fe$_2$As$_2$ (FeAs-122) single crystals. A pronounced kink is observed on the $H_{c1}(T)$ curve, which is attributed to the existence of two superconducting gaps. By fitting the data $H_{c1}(T)$ to the two-gap BCS model in full temperature region, a small gap of $\Delta_a(0)=2.0\pm 0.3$ meV and a large gap of $\Delta_b(0)=8.9\pm 0.4$ meV are obtained. The in-plane penetration depth $\lambda_{ab}(0)$ is estimated to be 105 nm corresponding to a rather large superfluid density, which points to the breakdown of the Uemura plot in FeAs-122 superconductors.Comment: 5 pages, 4 figure

Calcineurin B-Like Proteins CBL4 and CBL10 Mediate Two Independent Salt Tolerance Pathways in Arabidopsis.

In Arabidopsis, the salt overly sensitive (SOS) pathway, consisting of calcineurin B-like protein 4 (CBL4/SOS3), CBL-interacting protein kinase 24 (CIPK24/SOS2) and SOS1, has been well defined as a crucial mechanism to control cellular ion homoeostasis by extruding Na+ to the extracellular space, thus conferring salt tolerance in plants. CBL10 also plays a critical role in salt tolerance possibly by the activation of Na+ compartmentation into the vacuole. However, the functional relationship of the SOS and CBL10-regulated processes remains unclear. Here, we analyzed the genetic interaction between CBL4 and CBL10 and found that the cbl4 cbl10 double mutant was dramatically more sensitive to salt as compared to the cbl4 and cbl10 single mutants, suggesting that CBL4 and CBL10 each directs a different salt-tolerance pathway. Furthermore, the cbl4 cbl10 and cipk24 cbl10 double mutants were more sensitive than the cipk24 single mutant, suggesting that CBL10 directs a process involving CIPK24 and other partners different from the SOS pathway. Although the cbl4 cbl10, cipk24 cbl10, and sos1 cbl10 double mutants showed comparable salt-sensitive phenotype to sos1 at the whole plant level, they all accumulated much lower Na+ as compared to sos1 under high salt conditions, suggesting that CBL10 regulates additional unknown transport processes that play distinct roles from the SOS1 in Na+ homeostasis