Sustainable Pultruded Sandwich Profiles with Mycelium Core.

This research focuses on exploring the potential of mycelium as a sustainable alternative to wood or solid foam in pultruded glass fiber-reinforced plastic (GFRP) sandwich profiles. The study evaluates the performance and the environmental sustainability potential of this composite by mechanical tests and life cycle assessment (LCA). Analysis and comparison of pultruded sandwich profiles with mycelium, polyurethane (PUR) foam and chipboard demonstrate that mycelium is competitive in terms of its performance and environmental impact.

Recombinant peptide fusion construction for protein-templated catalytic palladium nanoparticles.

Although peptide-enabled synthesis of nanostructures has garnered considerable interest for use in catalytic applications, it has so far been achieved mostly via Fmoc based solid phase peptide synthesis. Consequently, the potential of longer peptides in nanoparticle synthesis have not been explored largely due to the complexities and economic constraints of this chemical synthesis route. This study examines the potential of a 45-amino acid long peptide expressed as fusion to green fluorescence protein (GFPuv) in Escherichia coli for use in palladium nanoparticle synthesis.

Development of a novel engineered E. coli host cell line platform with improved column capacity performance for ion-exchange chromatography.

This article reports on the analysis of an engineered Escherichia coli designed to reduce the host cell protein (HCP) burden on recombinant protein purification by column chromatography. Since downstream purification accounts for a major portion of production costs when using a recombinant platform, minimization of HCPs that are initially captured or otherwise interfere during chromatography will positively impact the entire purification process. Such a strategy, of course, would also require the cell line to grow, and express recombinant proteins, at levels comparable to, or better than, its parent strain.

Alternate carbohydrate and nontraditional inducer leads to increased productivity of a collagen binding domain fusion protein via fed-batch fermentation.

The production of collagen binding domain fusion proteins is of significant importance because of their potential as therapeutic biomaterials. It was previously reported that the expression of collagen-binding domain fusion proteins in Escherichia coli was higher when expressed using lactose as an inducer and chemically defined growth media on a shake flask scale. In an effort to further investigate factors that affect expression levels on a fed-batch scale, alternative induction techniques were tested in conjunction with fed-batch fermentation.

Expression of a collagen-binding domain fusion protein: effect of amino acid supplementation, inducer type, and culture conditions.

Collagen binding domain fusion proteins are of significant importance because of their potential as therapeutic biomaterials. In this paper, we investigate the production of such therapeutic proteins via fermentation of Escherichia coli on both an undefined medium and a defined medium. Defined media with amino acid supplementation provided higher amounts of therapeutic protein than undefined media with no supplementation.