The possibilities for surface hardening of titanium alloys by alloying with nitrogen are reviewed. Alloying has been carried out in the solid state by plasma nitriding and in the liquid state by laser melting in nitrogen. Microstructure, hardness profiles, and fatigue and wear properties have been examined. Wear resistance was found to be greatly improved by both techniques, although at the expense of a drop in fatigue properties. Case depths of 0.1 mm were produced by plasma nitriding, while 0.5 mm case depths and a maximum hardness of 1400 HV0.1 were achieved by laser alloying.

A series of thermal oxidising treatments has been carried out on V alloy at temperatures ranging from 600 to 850°C to develop a new surface engineering technique for Ti-6Al-4 V and other titanium alloys. Systematic characterisation of the thermal oxidation treated surface layers was performed using GDS, XRD, SEM, and nanoindentation testing. Ball on disc friction tests show that the coefficient offriction of a Ti-6Al-4 V disc against an alumina ball was significantly reduced after oxidation treatment. The rolling-sliding wear resistance of Timetal 6-4 material against hardened 709 M 40 steel under lubricated conditions has been

BackgroundAnimal-free recombinant proteins provide a safe and effective alternative to tissue or serum-derived products for both therapeutic and biomanufacturing applications. While recombinant insulin and albumin already exist to replace their human counterparts in cell culture media, until recently there has been no equivalent for serum transferrin.ResultsThe first microbial system for the high-level secretion of a recombinant transferrin (rTf) has been developed from Saccharomyces cerevisiae strains originally engineered for the commercial production of recombinant human albumin (Novozymes' Recombumin® USP-NF) and albumin fusion proteins (Novozymes' albufuse®). A full-length non-N-linked glycosylated rTf was secreted at levels around ten-fold higher than from commonly used laboratory strains. Modification of the yeast 2 μm-based expression vector to allow overexpression of the ER chaperone, protein disulphide isomerase, further increased the secretion of rTf approximately twelve-fold in high cell density fermentation. The rTf produced was functionally equivalent to plasma-derived transferrin.ConclusionsA Saccharomyces cerevisiae expression system has enabled the cGMP manufacture of an animal-free rTf for industrial cell culture application without the risk of prion and viral contamination, and provides a high-quality platform for the development of transferrin-based therapeutics.

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BackgroundSuccessful delivery of cell-based therapeutics into patients is compromised by their short shelf-life upon release from production facilities due to the living nature of the active component that rapidly loses viability, and therefore its properties. In this context, the use of appropriate additives may contribute to the stabilisation of the cellular component within specifications for a longer time until administration.ResultsIn the present study, we evaluated the effect of different formulations on the stability of viability, identity, and potency of clinical grade multipotent mesenchymal stromal cells in suspension, both electrolyte solution and protein content were found to impact on their shelf-life. Particularly cryopreservation of cells in a Plasmalyte 148 supplemented with 2% (w/v) AlbIX (a yeast-derived recombinant albumin) and 10% (v/v) dimethyl sulfoxide, and final formulation post-thawing in Plasmalyte 148 supplemented with 2% (w/v) AlbIX enabling prolonged stability from 24 h up to 72 h in optimal conditions. Further investigation on the mechanisms of action involved revealed a delay of apoptosis progression into late stage when AlbIX was present.ConclusionsThe use of optimal formulations for each cell type of interest is crucial to extend the shelf life of cell-based pharmaceuticals and contribute to solve logistical challenges. We demonstrated that the use of Plasmalyte 148 supplemented with 2% (w/v) AlbIX resulted in superior stability of multipotent mesenchymal stromal cells without affecting their identity and multipotency.Electronic supplementary materialThe online version of this article (10.1186/s12967-018-1659-4) contains supplementary material, which is available to authorized users.