The composition and rheological properties of beta-lactoglobulin/pectin coacervates have shown significant correlations with sodium chloride concentration (C(NaCl)) and initial protein/polysaccharide ratio (r). An increase of C(NaCl) from 0.01 to 0.21 M at r = 5:1 leads to the increase in both beta-lactoglobulin and pectin contents in the coacervates, which can be explained in terms of salt-enhanced effect at lower salt concentrations. Further increase of C(NaCl) from 0.21 to 0.41 M decreases the proportions of these two biopolymers in the coacervates, exhibiting salt-reduced effect at higher salt concentrations. Moreover, the stronger self-aggregation of beta-lactoglobulin with increasing salt concentration gives rise to a decreasing actual protein/polysaccharide ratio in the coacervates at 0.01-0.21 M C(NaCl) and r = 5:1. An increase of r from 5:1 to 40:1 often increases the actual amount of pectin chains in beta-lactoglobulin/pectin coacervates, but it exhibits a maximum in beta-lactoglobulin content at r = 20:1. A much higher storage modulus (G') than loss modulus (G' ') for all beta-lactoglobulin/pectin coacervates suggests the formation of highly interconnected gel-like structure. The values of G' increase as C(NaCl) increases from 0.01 to 0.21 M, whereas a further increase of C(NaCl) from 0.21 to 0.41 M causes G' values to decrease to much lower values. These results further disclose the salt-enhanced effect and the salt-reduced effect at low and high salt concentrations, respectively. On the other hand, increasing r from 5:1 to 40:1 favors the formation of stronger gel-like beta-lactoglobulin/pectin coacervates, which mainly originates from the higher actual amount of pectin chains in beta-lactoglobulin/pectin coacervates at higher r values.

Trans-cinnamaldehyde (TCA), an essential oil in cinnamon powder, may have beneficial effects as a treatment for stroke which is the second leading cause of death worldwide. Post-ischemic inflammation induces neuronal cell damage after stroke, and activation of microglia, in particular, has been thought as the main contributor of proinflammatory and neurotoxic factors. The purpose of this study was to investigate the neuroprotective effects of TCA in an animal model of ischemia/reperfusion (I/R)-induced brain injury and the neuroprotective mechanism was verified in LPS-induced inflammation of BV-2 microglial cells. Our results showed that TCA (10-30 mg/kg, p.o.) significantly reduced the infarction area, neurological deficit score and decreased iNOS and COX-2 protein expression level in I/R-induced injury brain tissue. It inhibited 0.5 µg/ml LPS-induced NO production in BV-2 microglial cells without affecting cell viability, reduced protein expression of iNOS and COX-2, and attenuated inhibition of p53 protein. TCA also suppressed the effects of LPS-induced nuclear translocation of NF-κB p65 and p50 and increased cytosolic IκBα. It also reduced LPS-induced mRNA expression of iNOS, COX-2, and TNFα. We concluded that TCA has a potential neuroprotective effect to against the ischemic stroke, which may be via the inhibition of neuroinflammation through attenuating iNOS, COX-2 expression and NF-κB signaling pathway.

Small-angle neutron scattering (SANS) has been used to investigate the microstructure of beta-lactoglobulin/pectin coacervates prepared by different initial protein/polysaccharide weight ratio (r), sodium chloride concentration (C(NaCl)), and pectin charge density. The higher r and higher pectin charge density lead to higher scattering intensity at small q range (0.007 Angstrom(-1) < q < 0.02 Angstrom(-1)), suggesting that the charges of pectin chains are screened significantly by the binding of oppositely charged protein molecules, leading to a tighter aggregation of pectin chains. On the other hand, the appearance of a shoulder peak at intermediate q range (0.04 Angstrom(-1) < q < 0.2 Angstrom(-1)) is used to interpret the formation of protein domains in beta-lactoglobulin/pectin coacervates. At C(NaCl) = 0.1 M, the coacervate of beta-lactoglobulin and pectin A does not show a shoulder peak at intermediate q range at r = 10:1, suggesting that protein molecules are separately bound on pectin chains. However, a shoulder peak appears at intermediate q range at r = 20:1 and 30:1, and the average protein domain size estimated from the shoulder peak position is 7.2 and 8.5 nm, respectively, for these two coacervates. When C(NaCl) increases from 0.05 to 0.2 M, the shoulder peak shifts toward smaller q and becomes broader, indicating that the addition of a higher amount of salt leads to a more heterogeneous coacervate structure. Pectin B with a lower linear charge density favors the formation of larger protein domains. The formation of protein domains in beta-lactoglobulin/pectin coacervates is partially ascribed to the self-aggregation of beta-lactoglobulin molecules. Two kinds of microstructures of beta-lactoglobulin/pectin coacervates with and without observable protein domains have been proposed.