Renliang Huang

Bioconversion of Lignocellulose into Bioethanol: Process Intensification and Mechanism Research

Biofuels produced from lignocellulosic biomass can significantly reduce the energy dependency on fossil fuels and the resulting effects on environment. In this respect, cellulosic ethanol as an alternative fuel has the potential to become a viable energy source in the near future. Over the past few decades, tremendous effort has been undertaken to make cellulosic ethanol cost competitive with conventional fossil fuels. The pretreatment step is always necessary to deconstruct the recalcitrant structures and to make cellulose more accessible to enzymes. A large number of pretreatment technologies involving physical, chemical, biological, and combined approaches have been developed and tested at the pilot scale. Furthermore, various strategies and methods, including multi-enzyme complex, non-catalytic additives, enzyme recycling, high solids operation, design of novel bioreactors, and strain improvement have also been implemented to improve the efficiency of subsequent enzymatic hydrolysis and fermentation. These technologies provide significant opportunities for lower total cost, thus making large-scale production of cellulosic ethanol possible. Meanwhile, many researchers have focused on the key factors that limit cellulose hydrolysis, and analyzing the reaction mechanisms of cellulase. This review describes the most recent advances on process intensification and mechanism research of pretreatment, enzymatic hydrolysis, and fermentation during the production of cellulosic ethanol.

Facile in situ synthesis of silver nanoparticles on procyanidin-grafted eggshell membrane and their catalytic properties.

Facile, efficient, and robust immobilization of metal nanostructures on porous bioscaffolds is an interesting topic in materials chemistry and heterogeneous catalysis. This study reports a facile in situ method for the synthesis and immobilization of small silver nanoparticles (AgNPs) at room temperature on natural eggshell membrane (ESM), which presents interwoven fibrous structure and can be used as a unique protein-based biotemplate. Procyanidin (Pro), a typical plant polyphenol extracted from grape seeds and skins, was first grafted onto ESM fibers to serve as both reductant and stabilizer during the synthesis process. As a result, the AgNPs were facilely synthesized and robustly immobilized on the ESM fibers without additional chemical reductant or physical treatments. The morphology and microstructure of the as-prepared AgNPs@Pro-ESM composites were characterized by combined microscopy and spectroscopy technologies. The results indicate that small AgNPs with mean diameter of 2.46 nm were successfully prepared on the Pro-ESM biotemplate. The composites exhibited good catalytic activity toward the reduction of 4-nitrophenol (4-NP). More importantly, these composite catalysts can be easily recovered and reused for more than eight cycles because of their high stability.

Self-assembling peptide–polysaccharide hybrid hydrogel as a potential carrier for drug delivery

Here we report a novel peptide–polysaccharide hybrid hydrogel as a potential carrier for sustained delivery of hydrophobic drugs. The hybrid hydrogel composed of Fmoc-diphenylalanine (Fmoc-FF) peptide and konjac glucomannan (KGM) was prepared through molecular self-assembly of Fmoc-FF in the KGM solution. The physicchemical properties of the Fmoc-FF–KGM hybrid hydrogel were further evaluated. This hybrid hydrogel exhibited a highly hydrated, rigid and nanofibrous gel network in which self-assembled peptide nanofibers were interwoven with the KGM chains. The results of a stability test and rheology study showed that the hybrid hydrogel has much higher stability and mechanical strength compared to Fmoc-FF hydrogel alone. Both CD and FTIR analysis indicated an anti-parallel β-sheet arrangement of Fmoc-FF peptide in self-assembled nanofibers, regardless the presence of KGM. Moreover, docetaxel was chosen as a model of hydrophobic drugs and incorporated into hydrogels to study the in vitro release behavior. The sustained and controlled drug release from this hybrid hydrogel was achieved by varying the KGM concentration, molecular weight, aging time or β-mannanase concentration. Our results not only provide a new strategy for fabricating Fmoc-FF–KGM hybrid hydrogel as a sustained-release drug carrier but also open an avenue for the design of new self-assembling peptide–polysaccharide hybrid hydrogels.

Rational Design of Chiral Nanostructures from Self-Assembly of a Ferrocene-Modified Dipeptide

We report a new paradigm for the rational design of chiral nanostructures that is based on the hierarchical self-assembly of a ferrocene (Fc)-modified dipeptide, ferrocene-L-Phe-L-Phe-OH (Fc-FF). Compared to other chiral self-assembling systems, Fc-FF is unique because of its smaller size, biocompatibility, multiple functions (a redox center), and environmental responsiveness. X-ray and spectroscopic analyses showed that the incorporation of counterions during the hierarchical self-assembly of Fc-FF changed the conformations of the secondary structures from flat β sheets into twisted β sheets. This approach enables chiral self-assembly and the formation of well-defined chiral nanostructures composed of helical twisted β sheets. We identified two elementary forms for the helical twist of the β sheets, which allowed us to create a rich variety of rigid chiral nanostructures over a wide range of scales. Furthermore, through subtle modulations in the counterions, temperature, and solvent, we are able to precisely control the helical pitch, diameter, and handedness of the self-assembled chiral nanostructures. This unprecedented level of control not only offers insights into how rationally designed chiral nanostructures can be formed from simple molecular building blocks but also is of significant practical value for the use in chiroptics, templates, chiral sensing, and separations.

Solvent and surface controlled self-assembly of diphenylalanine peptide: from microtubes to nanofibers

A new approach based on solvent and surface effects was developed for controlling the self-assembly of diphenylalanine peptide into microtubes and nanofibers. The HBD/HBA ability and surface tension may be major determinants in the formation of these peptide assemblies. Our results will lead to a better understanding of the molecular mechanisms involved in diphenylalanine self-assembly process.

Grafting hyaluronic acid onto gold surface to achieve low protein fouling in surface plasmon resonance biosensors.

Antifouling surfaces capable of reducing nonspecific protein adsorption from natural complex media are highly desirable in surface plasmon resonance (SPR) biosensors. A new protein-resistant surface made through the chemical grafting of easily available hyaluronic acid (HA) onto gold (Au) substrate demonstrates excellent antifouling performance against protein adsorption. AFM images showed the uniform HA layer with a thickness of ∼10.5 nm on the Au surface. The water contact angles of Au surfaces decreased from 103° to 12° with the covalent attachment of a carboxylated HA matrix, indicating its high hydrophilicity mainly resulted from carboxyl and amide groups in the HA chains. Using SPR spectroscopy to investigate nonspecific adsorption from single protein solutions (bovine serum albumin (BSA), lysozyme) and complex media (soybean milk, cow milk, orange juice) to an HA matrix, it was found that ultralow or low protein adsorptions of 0.6-16.1 ng/cm(2) (e.g., soybean milk: 0.6 ng/cm(2)) were achieved on HA-Au surfaces. Moreover, anti-BSA was chosen as a model recognition molecule to characterize the immobilization capacity and the antifouling performance of anti-BSA/HA surfaces. The results showed that anti-BSA/HA sensor surfaces have a high anti-BSA loading of 780 ng/cm(2), together with achieving the ultralow (<3 ng/cm(2) for lysozyme and soybean milk) or low (<17 ng/cm(2) for cow milk and 10% blood serum) protein adsorptions. Additionally, the sensor chips also exhibited a high sensitivity to BSA over a wide range of concentrations from 15 to 700 nM. Our results demonstrate a promising antifouling surface using extremely hydrophilic HA as matrix to resist nonspecific adsorption from complex media in SPR biosensors.

A polydopamine-modified optical fiber SPR biosensor using electroless-plated gold films for immunoassays.

A sensitive and stable electroless-plated gold film for the preparation of an optical fiber surface plasmon resonance (SPR) sensor is presented in this work, together with a facile antibody immobilization method. Gold nanoparticles were uniformly adsorbed onto the surface of an optical fiber forming a film with a thickness of approximately 56.3 nm. The sensor had a high sensitivity with 2054 nm/RIU and 3980 nm/RIU in the refractive index ranges of 1.333-1.359 and 1.359-1.386, respectively. An SPR biosensor was developed based on polydopamine-modified gold film (PDA-Au), which was fabricated by a simple and quick spontaneous polymerization of dopamine (DA) on the gold film. When goat anti-human IgG antibodies were immobilized, the PDA-Au surface had a larger resonant wavelength shift of 66.21 nm compared with the traditional 11-mercaptoundecanoic acid-modified gold film (MUA-Au) surface. In addition, the PDA-Au surface enabled the sensitive and selective determination of human IgG down to a concentration of 2 μg mL(-1) with a high sensitivity of 0.41 nm per μg mL(-1). The PDA-Au surface exhibited an approximately four fold higher sensitivity and an about seven fold lower LOD than the MUA-Au surface to human IgG.

Hierarchical, interface-induced self-assembly of diphenylalanine: formation of peptide nanofibers and microvesicles

To gain insight into the hierarchical self-assembly of peptides and the surface effect on assembly formation, an aromatic peptide of diphenylalanine (FF) was used in this study as the model peptide. We found that the diphenylalanine peptide could self-assemble into a core-branched nanostructure through non-covalent interactions in aqueous solution. The pre-assemblies further assembled into nanofibers and microvesicles on the glass surface and microporous membrane, respectively, showing a significant dependence on surface characteristics. The structural and morphological differences between nanofibers and microvesicles were investigated directly using several spectroscopy and microscopy techniques. Our results revealed a hierarchical and interface-induced assembly behavior of diphenylalanine peptide. The novel strategy based on the surface effect allows one to controllably fabricate various peptide-based nanostructures.

Understanding the key factors for enzymatic conversion of pretreated lignocellulose by partial least square analysis

The relationship between the physicochemical properties of lignocellulosic substrates and enzyme digestion is still not well known. After different pretreatments, cellulase hydrolysis and measurements of physicochemical characteristics by column solute exclusion, particle size analysis, X‐ray diffraction, Fourier transform infrared spectroscopy and solid state 13C nuclear magnetic resonance were performed in this study. Partial least squares was then applied to seek the key factors limiting the rate and extent of cellulose digestion. According to the PLS results, the most important factor for cellulose digestion was accessible interior surface area, followed by delignification and the destruction of the hydrogen bonds. The cellulose digestion at 2 and 24 hr were improved with the increased accessibility of interior surface area to the reporter molecules of 5.1‐nm diameter. Removal of lignin and breaking of hydrogen bonds were also found to significantly promote cellulose conversion. Other properties, including the breakdown of intramolecular hydrogen bonds, cellulose crystallinity, and hemicellulose content, had less effect on the efficiency of enzymatic hydrolysis.

Cross-linked lysozyme crystal templated synthesis of Au nanoparticles as high-performance recyclable catalysts

Bio-nanomaterials fabricated using a bioinspired templating technique represent a novel class of composite materials with diverse applications in biomedical, electronic devices, drug delivery, and catalysis. In this study, Au nanoparticles (NPs) are synthesized within the solvent channels of cross-linked lysozyme crystals (CLLCs) in situ without the introduction of extra chemical reagents or physical treatments. The as-prepared AuNPs-in-protein crystal hybrid materials are characterized by light microscopy, transmission electron microscopy, x-ray diffraction, and Fourier-transform infrared spectroscopy analyses. Small AuNPs with narrow size distribution reveal the restriction effects of the porous structure in the lysozyme crystals. These composite materials are proven to be active heterogeneous catalysts for the reduction of 4-nitrophenol to 4-aminophenol. These catalysts can be easily recovered and reused at least 20 times because of the physical stability and macro-dimension of CLLCs. This work is the first to use CLLCs as a solid biotemplate for the preparation of recyclable high-performance catalysts.