Journal Articles

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Subject: search.filters.subject.290000 Engineering and Technology

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    Exploring The Responsibilities Of Single-Inhabitant Smart Homes With Use Cases
    (IOS Press, 2010) Lyons P; Tran CA; Steinhauer HJ; Marsland S; Dietrich J; Guesgen HW
    This paper makes a number of contributions to the field of requirements analysis for Smart Homes. It introduces Use Cases as a tool for exploring the responsibilities of Smart Homes and it proposes a modification of the conventional Use Case structure to suit the particular requirements of Smart Homes. It presents a taxonomy of Smart-Home-related Use Cases with seven categories. It draws on those Use Cases as raw material for developing questions and conclusions about the design of Smart Homes for single elderly inhabitants, and it introduces the SHMUC repository, a web-based repository of Use Cases related to Smart Homes that anyone can exploit and to which anyone may contribute.
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    Recent advances in technologies for vitamin A protection in foods.
    (Elsevier, 2008) Loveday, SM; Singh, Harjinder
    Vitamin A deficiency affects many children in the developing world, and is preventable via food or pharmaceutical supplementation. The main technical barrier to the fortification of food with vitamin A is its susceptibility to oxidation and isomerization, which result in loss of nutritional efficacy. This review discusses recent technological avenues for stabilizing vitamin A in foods.
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    Physicochemical changes in a model protein bar during storage
    (Elsevier, 2009) Loveday, SM; Hindmarsh, Jason; Creamer, Lawrence K; Singh, Harjinder
    High-protein snack bars (protein bars) contain high-quality protein, sugars and other low molecular weight polyhydroxy compounds (PHCs), high-energy confectionary fats, and a minimum of water (water activity ≤ 0.65). The consequence of the intimate mixing of these components in protein bars is that they can react together, creating sensory characteristics that are unacceptable to consumers. This study examined the changes occurring in a model protein bar during storage for 50 days at 20 °C. Over this time, fracture stress increased from 20.1 +/- 1.8 Pa to 201 +/- 75 Pa at a rate that decreased slightly over time. 1H nuclear magnetic resonance (NMR) showed that the molecular mobility of PHCs decreased dramatically over the first 5 days as the batter set into a solid bar. Over the first 17 hours after manufacturing, protein particles became more clustered, and soluble protein appeared to precipitate, as shown by confocal microscopy. Reactive lysine fell 38% in the first 10 days of storage and was approximately constant thereafter. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed little change in protein molecular weights. Following the initial ‘setting’ phase of 5-10 days, fracture stress continued to increase and the molecular mobility of PHCs decreased. Changes in PHC molecular mobility were consistent with glucose crystallisation. Chemical changes were minimal during this phase, which suggests that chemical reactions play little part in the hardening of protein bars and that changes in molecular mobility and changes in microstructure driven by moisture migration may be more important.
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    Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment
    (Cambridge University Press, 2001) Havea P; Singh H; Creamer LK
    Bovine b-lactoglobulin (b-lg), a-lactalbumin (a-la) and bovine serum albumin (BSA), dispersed in ultra®ltration permeate, that had been prepared from whey protein concentrate solution (100 g}kg, pH 6±8), were heated at 75 °C. The consequent protein aggregation was studied by one-dimensional (1D) and twodimensional (2D) polyacrylamide gel electrophoresis (PAGE). When 100 g b-lg}kg permeate solution was heated at 75 °C, cooled and examined, large aggregates were observed. These aggregates were partially dissociated in SDS solution to give monomers, disulphide-bonded dimers, trimers and larger aggregates. When mixtures of b-lg and a-la or BSA were heated, homopolymers of each protein as well as heteropolymers of these proteins were observed. These polymer species were also observed in a heated mixture of the three proteins. Two-dimensional PAGE of mixtures demonstrated that these polymers species contained disulphide-bonded dimers of b-lg, a-la and BSA, and 1:1 disulphide-bonded adducts of a-la and b-lg, or BSA. These results are consistent with a mechanism in which the free thiols of heattreated b-lg or BSA catalyse the formation of a range of monomers, dimers and higher polymers of a-la. It is likely that when whey protein concentrate is heated under the present conditions, BSA forms disulphide-bonded strands ahead of b-lg and that a-la aggregation with b-lg and with itself is catalysed by the heat-induced unfolded BSA and b-lg.