RESUMO
The physicochemical and functional properties of tree peony seed protein were investigated. Tree peony seed protein with a favourable amino acid profile was composed of a 60kDa protein with two subunits of 38 and 23kDa. The isoelectric points of the two subunits were 3.6 and 9.0. Moreover, acid-Schiff staining indicated both of them were glycoproteins. Diagonal and 2-D electrophoresis data indicated the 38kDa subunit included three types, which two types had inter-disulphide bonds and one type had no-disulphide bonds. So did the 23kDa subunit. Circular dichroism spectra indicated the tree peony seed protein had predominantly a ß-sheet structure. Differential scanning calorimetry analysis indicated the denaturation temperatures of the tree peony seed protein at pH 5.0, 7.0 and 9.0 were 92.0, 97.1 and 95.2°C, respectively. Tree peony seed protein could be a food ingredient in the food industry due to its desirable physicochemical and functional properties.
Assuntos
Paeonia , Fenômenos Químicos , Sementes , ÁrvoresRESUMO
We report a detailed investigation on the lower critical field H{c1} of the superconducting Ba0.6K0.4Fe2As2 (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 the full temperature region, a small gap of Delta{a}(0)=2.0+/-0.3 meV and a large gap of Delta{b}(0)=8.9+/-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 122 superconductors.
