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This paper presents an innovative comparison that works creatively with the entangled spatialities of policy mobilities, drawing on a city-to-city cooperation between São Paulo (Brazil) and eThekwini (South Africa) municipalities for the exchange of slum upgrading expertise. The proposed comparative tactic entails tracing the establishment of this connection in order to disassemble the constituent flows and localities merged within it. Subsequently, by posing questions to one another, a relational comparison of the trajectory of slum upgrading policy in each locality is composed, unearthing the political and institutional conditions that preceded the existence of the connection per se. In that sense, both eThekwini and São Paulo are considered equivalent starting points from which local actors engaged in circulating ideas and mobilised slum upgrading policies. This paper not only brings a fresh approach to comparative methods – incorporating political contexts and their extensive overlapping networks of relations alongside a focus on particular policy trajectories – but also contributes to furthering global urban studies in two other ways. First, it provides insight into the processes by which policies are put on the move and localised (or not). Second, it demonstrates how repeated instances of urban practice may be unravelled by allowing each context of policy formation, with its distinctive trajectory of slum upgrading, to speak to one another. In this regard, the comparative analysis identified how, in both São Paulo and eThekwini, the consolidation of democracy was followed by the development of more technocratic approaches to the detriment of earlier slum upgrading initiatives focussed on community empowerment. [ABSTRACT FROM AUTHOR]

Combination of β-lactoglobulin (β-Lg) and lactoferrin (Lf), biomacromolecules derived from bovine whey, was used in the formation of supramolecular structures by thermal gelation technique to adjust the pH. Furthermore, the influence of the molar ratio, temperature, pH, and heating time in the formation of supramolecular structures were also studied. The characterization of the protein supramolecular structures was performed using dynamic light scattering, zeta potential measurements, molecular spectrofluorimetry, and circular dichroism spectroscopy. The thermal behavior of the pure proteins was investigated by differential scanning calorimetry. The protein denaturation temperatures were of around 85 °C for the β-Lg and around 52 °C and 85 °C (a small portion) for the Lf. The protein molar ratio of 2:1 Lf/β-Lg was used to form the structures, whose characterization showed that the best conditions of supramolecular structure formation occurred at pH 6.5 and at temperatures of 62.5 °C. In those conditions, more stable systems with reduced hydrophobic surface and average sizes between 30 and 100 nm were generated. The correlation between pH and temperature suggests that the method of preparation of the supramolecular structure affects its size during storage. [ABSTRACT FROM AUTHOR]