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  • Barth, Henrik, 1971-, et al. (författare)
  • Sustainable Development for Food Waste : A Case Study of Catered Meal Service at Schools and Elderly Care homes
  • 2019
  • Ingår i: Journal of Strategic Innovation and Sustainability. - West Palm Beach, FL : North American Business Press. - 1718-2077. ; 14:2, s. 21-34
  • Tidskriftsartikel (refereegranskat)abstract
    • Food waste is an important topic in the context of sustainable development. Although many studies have addressed this topic, there is still limited knowledge owing to insufficient data. This study reports on food waste in two institutional settings in a Swedish municipality: schools and elderly care homes. The findings suggest it is easier to measure and reduce food waste in stable environments, such as exist at schools, than at environments characterized by change and unpredictability, such as exist at elderly care homes. Specific areas examined and compared include cooking and receiving kitchens, infrastructure, communications, and support. © North American Business Press.
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  • Ulvenlund, Stefan, et al. (författare)
  • Hydrophobic homopolymers of native α-L-amino acids at the air-water interface : A study by circular dichroism spectroscopy, atomic force microscopy, and surface balance experiments
  • 2001
  • Ingår i: Journal of Colloid and Interface Science. - : Elsevier BV. - 0021-9797. ; 242:2, s. 346-353
  • Tidskriftsartikel (refereegranskat)abstract
    • Films of poly-L-leucine, poly-L-valine, and poly-L-isoleucine have been studied at the air-water interface by surface balance experiments. In addition, Langmuir-Blodgett (LB) films of these polypeptides deposited onto quartz and mica have been studied by circular dichroism (CD) spectroscopy and atomic force microscopy (AFM) to elucidate the effects of polypeptide conformation and spreading agent (chloroform and trifluoroacetic acid, TFA) on film morphology and phase behavior. Monolayers of poly-L-leucine contain α-helical polypeptide strands. When spread from chloroform, the compression isotherm displays a collapse plateau and a limiting molecular area (A0) of 19 Å2 per amino acid residue. The corresponding LB films are flat and featureless. When a water-soluble solvent (TFA) is used as a spreading agent, the AFM results reveal an extensive formation of polypeptide aggregates. The aggregation is accompanied by a substantial decrease in A0 but has little effect on polypeptide conformation, film compressibility, and phase behavior. According to CD spectroscopy, films of poly-L-valine and poly-L-isoleucine contain polypeptide strands in β-sheet conformation. The corresponding isotherms are steep and lack a collapse plateau. When TFA is used as a spreading agent, the limiting area decreases, but AFM data do not give direct evidence for any aggregation.
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