Search

Electron beam freeform fabrication is a wire feed direct energy deposition additive manufacturing process, where the vacuum condition ensures excellent shielding against the atmosphere and enables processing of highly reactive materials. In this work, this technique is applied for the α + β-titanium alloy Ti-6Al-4V to determine suitable process parameter for robust building. The correlation between dimensions and the dilution of single beads based on selected process parameters, leads to an overlapping distance in the range of 70%-75% of the bead width, resulting in a multi-bead layer with a uniform height and with a linear build-up rate. Moreover, the stacking of layers with different numbers of tracks using an alternating symmetric welding sequence allows the manufacturing of simple structures like walls and blocks. Microscopy investigations reveal that the primary structure consists of epitaxial grown columnar prior β-grains, with some randomly scattered macro and micropores. The developed microstructure consists of a mixture of martensitic and finer α-lamellar structure with a moderate and uniform hardness of 334 HV, an ultimate tensile strength of 953 MPa and rather low fracture elongation of 4.5%. A subsequent stress relief heat treatment leads to a uniform hardness distribution and an extended fracture elongation of 9.5%, with a decrease of the ultimate strength to 881 MPa due to the fine α-lamellar structure produced during the heat treatment. Residual stresses measured by energy dispersive X-ray diffraction shows after deposition 200-450 MPa in tension in the longitudinal direction, while the stresses reach almost zero when the stress relief treatment is carried out.

The intermediate filament protein, desmin, was purified from pork longissimus dorsi and incubated with either μ-calpain, m-calpain or cathepsin B. Proteolysis of desmin was followed using SDS-PAGE and Western blotting. After incubation of desmin with the proteases, cleavage sites on the desmin molecule were identified by N-terminal sequencing of the different proteolytic fragments. Desmin incubated with either m-calpain or μ-calpain was primarily cleaved in the head and tail region leaving the rod domain relatively intact even after prolonged incubation. Incubation with cathepsin B produces a sequential C-terminal degradation pattern characteristic of this dipeptylpeptidase. The substrate primary structure was not found to be essential for regulation of the proteolytic activity of the cysteine peptidases studied. However, the degradation patterns obtained imply that calpains are involved in degradation of desmin early post-mortem, targeting the non-helical region of the desmin molecule and resulting in depolymerisation and initial disorganisation of the intermediate filament structures of the muscle cell.

We exhibit a situation in which cosmological perturbations of astrophysical relevance propagating through a bounce are affected in a scale-dependent way. Involving only the evolution of a scalar field in a closed universe described by general relativity, the model is consistent with causality. Such a specific counterexample leads to the conclusion that imposing causality is not sufficient to determine the spectrum of perturbations after a bounce provided it is known before. We discuss consequences of this result for string motivated scenarios.

Nuclear magnetic resonance (NMR) measurements were carried out on pork longissimus muscle, which pre rigor had been manipulated to various muscle lengths, to investigate the relationship between the microstructure of meat and the NMR T(2) relaxation. Distributed exponential analysis of the NMR T(2) relaxation data revealed the existence of three distinct water populations: T(2b), T(21), and T(22). A high, significant correlation was found between the T(21) time constant and the sarcomere length (r = 0.84) and calculated ration of myofilament lattice volume in the I-band and A-band regions, respectively (r = 0.84), considering sigmoid relationships. The result implies that the T(21) time constant mainly is determined by the structure of the myofilament lattice and so strongly supports a previously proposed theory that the T(21) population corresponds to water located within a highly organized myofibrillar protein matrix including actin and myosin filament structures. A high correlation was also found between the T(22) population and the water-holding capacity (WHC) (r = 0.76), which suggests that the WHC is mainly determined by the amount of loosely bound extramyofibrillar water. However, the correlation between NMR T(2) parameters and WHC was further increased (r = 0.84) by including the T(21) time constant in the correlation analysis. This implies that the formation of drip loss is an ongoing process involving the transfer of water from myofibrils to the extracellular space and is affected by structural features at several levels of organization within the muscle tissue. This study demonstrates the advantages of NMR T(2) relaxation as an effective technique for obtaining further understanding of the relationship between the microstructure of meat, its WHC, water mobility, and water distribution.