A recent increase in the use of biofibers as low-cost and renewable reinforcement for the polymer biocomposites has been seen globally. Biofibers are classified into: lignocellulosic fibers (i.e., cellulose, wood and natural fibers), nanocellulose (i.e., cellulose nanocrystals and cellulose nanofibrils), and bacterial cellulose, while polymer matrix materials can be petroleum based or bio-based. Green biocomposites can be produced using both biobased fibers and polymers. Incompatibility between the hydrophilic biofibers and hydrophobic polymer matrix can cause performance failure of resulting biocomposites. Diverse efforts have focused on the modification of biofibers in order to improve the performances of biocomposites. “Grafting” copolymerization strategy can render the advantages of biofiber and impart polymer properties onto it and the performance of biocomposites can be tuned through changing grafting parameters. This review presents a short overview of various “grafting” methods which can be directly or potentially employed to enhance the interaction between biofibers and a polymer matrix for biocomposites. Major grafting techniques, including ring opening polymerization, grafting via coupling agent and free radical induced grafting, have been discussed. Improved properties such as mechanical, thermal, and water resistance have provided grafted biocomposites with new opportunities for applications in specific industries.

In this study, α-cellulose fibers reinforced green biocomposites based on polyhydroxybutyrate (PHB) and the copolymer poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV) were prepared and characterized. The α-cellulose fibers were isolated from at-risk intermountain lodgepole pine wood by successive removal of extractives, lignin and hemicellulose. Grafting of PHB or PHBV onto cellulose was conducted using reactive extrusion with dicumyl peroxide free radical initiation at high temperature. It is postulated that the grafted copolymers at the interfaces of cellulose and the polymer matrix performed as an interfacial coupling agent. Grafting tended to interact with both the hydrophilic fibers and the hydrophobic PHB or PHBV matrix. The biocomposites were characterized by scanning electron microscopy (SEM) and dynamic mechanical analysis (DMA) and indicated good interfacial bonding and compatibility between the two phases. The mechanical properties of the biocomposites were improved by grafting due to improved stress transfer between the two interphases of the fiber/polymer matrix as compared to the blend control composite. The crystallinity of PHB, PHBV and cellulose in the biocomposite were reduced as determined by Fourier transform infrared spectroscopy (FTIR), wide-angle X-ray diffraction (WAXD), and differential scanning calorimetry (DSC) analyses. This in situ reactive extrusion process offers an effective approach to improve the properties of biocomposite materials from sustainable resources.

Complete structures, including the location of N‐acetylneuraminic acid (Neu5Ac) residues, were assigned for the core regions of Campylobacter jejuni serotypes O:1, O:4, and O:23 and O:36 lipopolysaccharides (LPS). In continuation of earlier studies, structure determinations of liberated oligosaccharides and, where necessary, of intact LPS, were by ¹H‐NMR spectroscopy, Smith degradation, chromium trioxide and enzymic degradations, in conjunction with methylation studies supported by fast‐atom‐bombardment mass spectrometry and linkage analyses by gas chromatography/mass spectrometry. It was concluded on the basis of the following structures, in which each was linked 1→5 to a terminal 3‐deoxy‐D‐manno‐octulosonic acid residue, that the core regions with qualititatively similar sugar compositions showed serotypic differences in one or more of their sequences, linkage types, and anomeric configurations: image The outer regions of each structure carry Neu5Ac residues linked 2→3 to available β‐D‐Galp residues and show striking similarities with various glycosphingolipids of the ganglioside family. However, Neu5Ac epitopes are not apparently involved in determining serospecificity.