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Functional polymeric materials composed solely of lignin preparations appeared only very recently. A gradual paradigm shift spanning 56 years has revealed how lignin-lignin blends can upgrade the performance of 100 wt% lignin-based plastics. The view, first espoused in 1960, that lignin macromolecules are crosslinked reduces the plausibility of creating functional polymeric materials that are composed only of lignin preparations. Lignin-based materials would be much weaker mechanically if interstices remain in significant numbers between adjoining macromolecular structures that consist of rigid crosslinked chains. In 1982, random-coil features in the hydrodynamic character of kraft lignin (KL) components were evident from ultracentrifugal sedimentation equilibrium studies of their SEC behavior. In 1997, it was recognized that the macromolecular species in plastics with 85 wt% levels of KL are associated complexes rather than individual components. Finally, in 2016, the first polymeric material composed entirely of ball-milled softwood lignin (BML) was found to support a tensile strength above polyethylene. Except in its molecular weight, the BML was similar in structure to the native biopolymer. It was composed of associated lignin complexes, each with aromatic rings arranged in two domains. The inner domain maintains structural integrity largely through noncovalent interactions between cofacially-offset aromatic rings; the peripheral domain contains a higher proportion of edge-on aromatic-ring arrangements. Interdigitation between peripheral domains in adjoining complexes creates material continuity during casting. By interacting at low concentrations with the peripheral domains, non-lignin blend components can improve the tensile strengths of BML-based plastics to values well beyond those seen in polystyrene. The KL-based plastics are weaker because the peripheral domains of adjoining complexes are less capable of interdigitation than those of BML. Blending with 5 wt% 1,8-dinitroanthraquinone results in a tensile strength above that of polyethylene. Analogous effects can be achieved with 10 wt% maple γ-valerolactone (GVL) lignin which, with a structure close to the native biopolymer, imparts some native character to the peripheral domains of the KL complexes. Comparable enhancements in the behavior of BML complexes upon blending with 10 wt% ball-milled corn-stover lignin (BMCSL) result in lignin-only polymeric materials with tensile strengths well beyond polystyrene.

Lignins upgrade the lignocellulosic cell-wall domains in all vascular plants; they embody 20-30% of terrestrial organic carbon. For 50 years, mistaken assumptions about the configuration of lignin have hindered the development of useful polymeric materials with a lignin content above 40 wt%. Now, polymeric materials composed only of methylated softwood lignin derivatives can exhibit better tensile behavior than polystyrene. Marked improvements may be achieved with small quantities (5-10 wt%) of miscible blend components as simple as poly(ethylene glycol). These observations contradict commonly held views about crosslinking or hyper-branching in lignin chains. The hydrodynamic compactness of the macromolecular lignin species arises from powerful noncovalent interactions between the lignin substructures. Individual lignin components undergo association to form macromolecular complexes that are preserved in plastics with a very high lignin content. Material continuity results from interpenetration between the peripheral components in adjoining lignin complexes. Through interactions with the peripheral domains, miscible blend components modulate the strength and ductility of these utterly original lignin-based plastics.

Over the past three decades, the activities of four kinds of enzyme have been purported to furnish the mechanistic foundations for macromolecular lignin depolymerization in decaying plant cell walls. The pertinent fungal enzymes comprise lignin peroxidase (with a relatively high redox potential), manganese peroxidase, an alkyl aryl etherase, and laccase. The peroxidases and laccase, but not the etherase, are expressed extracellularly by white-rot fungi. A number of these microorganisms exhibit a marked preference toward lignin in their degradation of lignocellulose. Interestingly, some white-rot fungi secrete both kinds of peroxidase but no laccase, while others that are equally effective express extracellular laccase activity but no peroxidases. Actually, none of these enzymes has been reported to possess significant depolymerase activity toward macromolecular lignin substrates that are derived with little chemical modification from the native biopolymer. Here, the assays commonly employed for monitoring the traditional fungal peroxidases, alkyl aryl etherase, and laccase are described in their respective contexts. A soluble native polymeric substrate that can be isolated directly from a conventional milled-wood lignin preparation is characterized in relation to its utility in next-generation lignin-depolymerase assays.

Lignins play a crucial role in the cell-wall architecture of all vascular plants. They are composed of p-hydroxyphenylpropanoid units interconnected through covalent bonds formed during lignol radical coupling between six different pairs of atomic centers. For 50years, the primary structures of lignins have been thought to be random, but for a number of reasons such an assumption is not tenable. For example, it has been reported that, by simple physicochemical means, the rather recalcitrant lignins in spruce wood can be decisively separated into two fractions containing quite dissimilar biopolymer chains. Thus, a paradigm shift should be imminent, and a detailed working hypothesis for the mechanism of lignin biosynthesis would be invaluable in delineating how the process of macromolecular lignin assembly can be properly investigated. In conjunction with an earlier experimental result, an explicit model for a template dehydropolymerization process has been developed that describes how lignin primary structure is replicated. The strengths of the powerful noncovalent interactions have been calculated that control the transient placement of lignol radicals about to undergo coupling on a double-stranded lignin template. These elementary steps engender, in the growing daughter chain, a primary structure identical to that of the distal template strand. The interactions are governed by dynamical electron correlation in the pi-orbitals of each immobilized lignol radical and the complementary aromatic ring in the antiparallel proximal strand. The resulting noncovalent forces are computed to be stronger than those stabilizing GC/CG base pairs in DNA double-helices, but the mechanism of replication is fundamentally different from that of any other biopolymer., (Copyright 2009 Elsevier Ltd. All rights reserved.)

The regio- and stereospecificity of bimolecular phenoxy radical coupling reactions, of especial importance in lignin and lignan biosynthesis, are clearly controlled in some manner in vivo; yet in vitro coupling by oxidases, such as laccases, only produce racemic products. In other words, laccases, peroxidases, and comparable oxidases are unable to control regio- or stereospecificity by themselves and thus some other agent must exist. A 78-kilodalton protein has been isolated that, in the presence of an oxidase or one electron oxidant, effects stereoselective bimolecular phenoxy radical coupling in vitro. Itself lacking a catalytically active (oxidative) center, its mechanism of action is presumed to involve capture of E-coniferyl alcohol-derived free-radical intermediates, with consequent stereoselective coupling to give (+)-pinoresinol.