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The influence of the main-chain liquid crystalline polyester (PBDPS) on the crystallization and melting behaviors of isotactic polypropylene (iPP) has been investigated by differential scanning calorimetry (DSC), X-ray diffraction (WAXD), and polarized optical microscopy (POM). The results suggested that PBDPS is an efficient β-nucleating agent for iPP. The melting crystallization temperature as well as β-crystal of iPP increased with increasing of PBDPS content. The relative content of β-iPP crystals (k β) can reach 96.6% while adding 4% PBDPS during isothermal crystallization at 135 °C. The increased β-nucleation efficiency was ascribed to the adjacent phenyl rings in side groups of PBDPS stacked well together even when the temperature was higher than its clearing point (T i). Moreover, the distance between stacked phenyls is 0.32 nm, which is half of the unit cell parameter in the c-direction of β-iPP, indicating a lattice match between β-iPP and PBDPS.

Abstract:Lignin is a natural biopolymer with a complex three-dimensional network. It is the second most abundant natural polymer on earth. Commercially, lignin is largely obtained from the waste liquors of pulping and bioethanol productions. In this study, wheat straw alkali lignin (WSAL) was demethylated by using an in-situ generated Lewis acid under an optimized demethylation process. The demethylation process was monitored by a semi-quantitative Fourier Transform Infrared Spectroscopy (FTIR) method. The demethylated wheat straw alkali lignin (D-WSAL) was further characterized by Proton Nuclear Magnetic Resonance ( 1 H NMR), Gel Permeation Chromatography (GPC), and titration methods. After the demethylation process, it was found that the relative value of the methoxy group decreased significantly from 0.82 to 0.17 and the phenolic hydroxyl group increased from 5.2% to 16.0%. Meanwhile, the hydroxyl content increased from 6.6% to 10.3%. GPC results suggested that the weighted averaged molecular weight of D-WSAL was lower than that of WSAL with a smaller polydispersity index. The D-WSAL was then used to replace 60 wt % of phenol to prepare lignin-based phenol formaldehyde adhesives (D-LPF). It was found that both the free formaldehyde content and the free phenol content in D-LPF were less than those of the lignin-based phenol formaldehyde adhesives without lignin demethylation (LPF). Gel time of D-LPF was shortened. Furthermore, the wet and dry bonding strengths of lap shear wood samples bonded using D-LPF were higher than those of the samples bonded using LPF. Therefore, D-WSAL has shown good potential for application in phenol formaldehyde adhesives.

Soybean allergy is a serious health risk to humans and animals; β-conglycinin is the primary antigenic protein in soybean. Intestinal porcine epithelial (IPEC-J2) cells were used as an in vitro physiological model of the intestinal epithelium to study the effects of different concentrations of soybean antigen protein β-conglycinin to identify the involved signaling pathways. The cells were divided into eight groups and either untreated or treated with different concentrations of β-conglycinin, pyrrolidine dithiocarbamate (PDTC), N ω -nitro-L-arginine methyl ester hydrochloride (L-NAME), SP600125, and SB202190 either alone or in combination. The cells were incubated with 1, 5, and 10 mg•mL −1 β-conglycinin or 5 mg•mL −1 β-conglycinin and 1 μmol•L −1 nuclear factor κB (NF-κB) inhibitor (PDTC), inducible nitric oxide synthase inhibitor (L-NAME), c-Jun N-terminal kinase (JNK) inhibitor (SP600125), and p38 inhibitor (SB202190) for 24 h, separately; controls were left untreated. The mRNA, protein, and phosphorylation levels of NF-κB, p38, and JNK were higher in the treated groups than in the control group. β-Conglycinin decreased tight junction distribution, destroyed the cytoskeleton of IPEC-J2 cells, and caused cell death. After the addition of the inhibitors, β-conglycinin-induced IPEC-J2 cell damage was significantly reduced. β-Conglycinin caused damage to IPEC-J2 cells via the mitogen-activated protein kinase/NF-κB signaling pathway. The results of this study are crucial for exploring the mechanisms underlying allergic reactions caused by soybean antigen proteins.