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  • 1
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    Support to Regional Aquatic Resources Management (STREAM) | Bangkok, Thailand
    In:  http://aquaticcommons.org/id/eprint/2308 | 424 | 2011-09-29 19:16:30 | 2308 | Support to Regional Aquatic Resources Management
    Publication Date: 2021-07-13
    Description: The purpose of the project was to investigate international trade in fisheries products and its relationship to poverty alleviation and livelihoods of poor aquatic resource users in developing countries in Asia, and to identify options to improve the effectiveness of poverty reduction through international seafood trade. The project directly addressed the EC-PREP priority area of trade and development, and indirectly provided valuable insight to two other priority areas: food security and sustainable rural development; and institutional capacity building. [PDF contains 60 pages.]
    Description: International seafood trade: supporting sustainable livelihoods among poor aquatic resource users in Asia (EC PREP Project EP/RO3/R14)
    Description: The STREAM Initiative was hosted at the Network of Aquaculture Centres in Asia-Pacific (NACA) in Bangkok (Thailand)
    Keywords: Fisheries ; Sociology ; Policies ; South-East Asia ; Indonesia ; Philippines ; Vietnam
    Repository Name: AquaDocs
    Type: monograph
    Format: application/pdf
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  • 2
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    Support to Regional Aquatic Resources Management (STREAM) | Bangkok, Thailand
    In:  http://aquaticcommons.org/id/eprint/1437 | 6 | 2011-09-29 20:37:25 | 1437 | Support to Regional Aquatic Resources Management
    Publication Date: 2021-07-08
    Description: (121 p.)
    Description: The International Seafood Trade: Supporting Sustainable Livelihoods Among Poor Aquatic Resource Users in Asia (EC-PREP Project EP/R03/014)
    Description: The Stream Initiative was hosted at the Network of Aquaculture Centres in Asia-Pacific (NACA). The report should be referenced as: Macfadyen, G., Banks, R, Phillips, M, Haylor, G., Mazaudier, L. and Salz, P. 2003. Output 1 Background paper on the International Seafood Trade and Poverty. Prepared under the DFID-funded ECPREP project (EP/R03/014) “International Seafood Trade: Supporting Sustainable Livelihoods Among Poor Aquatic Resource Users in Asia”. Poseidon Aquatic Resource Management Ltd (UK), Network of Aquaculture Centres in Asia-Pacific and STREAM Initiative. Internet version available at www.enaca.org
    Keywords: Fisheries ; Sociology ; seafood trade ; poverty ; economics
    Repository Name: AquaDocs
    Type: monograph
    Format: application/pdf
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  • 3
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    WorldFish | Penang, Malaysia
    In:  http://aquaticcommons.org/id/eprint/18467 | 115 | 2015-10-28 07:40:12 | 18467 | WorldFish Center
    Publication Date: 2021-07-09
    Description: Aquaculture is the fastest-growing food production sector globally, with production projected to double within the next 15–20 years. Future growth of aquaculture is essential to providing sustainable supplies of fish in national, regional and global fish food systems; creating jobs; and maintaining fish at affordable levels for resource-poor consumers. To ensure that the anticipated growth of aquaculture remains both economically and ecologically sustainable, we need to better understand the likely patterns of growth, as well as the opportunities and challenges, that these trends present. This knowledge will enable us to better prioritize investments that will help ensure the sustainable development of the sector. In Indonesia, WorldFish and partners have applied a unique methodology to evaluate growth trajectories for aquaculture under various scenarios, as well as the opportunities and challenges these represent. Indonesia is currently the fourth largest aquaculture producer globally, and the sector needs to grow to meet future fish demand. The study overlapped economic and environmental models with quantitative and participatory approaches to understand the future of aquaculture in Indonesia. Such analyses, while not definitive, have provided new understanding of the future supply and demand for seafood in Indonesia stretching to 2030. The learning from this research provides a foundation for future interventions in Indonesian fish food systems, as well as a suite of methodologies that can be applied more widely for insightful analyses of aquaculture growth trajectories in other countries or regions.
    Description: Gordon and Betty Moore Foundation
    Description: CGIAR Research Programs on Policies, Institutions and Markets
    Description: CGIAR Research Programs on Livestock and Fish
    Keywords: Aquaculture ; Fisheries ; Aquaculture ; Fisheries ; Research ; Asia ; Indonesia
    Repository Name: AquaDocs
    Type: monograph
    Format: application/pdf
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    Format: 16
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 14 (1975), S. 1995-2005 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The changes in conformation undergone by α-gelatin molecules on quenching aqueous solutions to below the temperature at which they can gel have been monitored by nuclear magnetic resonance and dielectric relaxation techniques. The relative rates of these conformational transitions are compared with changes in rheological properties. The nmr spectral intensity changes for 0.2 and 0.5% w/v α-gelatin solutions correspond to a unimolecular process with k ∼ 10-2 min-1 at 15°C; this process occurs independently of whether or not the solution is concentrated enough to form a gel. The process involves a slow intramolecular nucleation step, followed by a rapid conformational change of the whole molecule from random coil to a rigid stage. Comparison with other data suggests that the transition gives rise to a triple collagen-like helix. In dilute solution (but above the critical concentration for gel formation, e.g., 0.5% w/v), the gelatin process follows the formation of the rigid molecular species. It probably involves the formation of junction zones consisting of three polypeptide chains in a collagen-like triple-helical conformation. These junctions may form, at low concentrations, from a reorganization of previously formed, intramolecular, triple helices. Solutions below a concentration of about 0.4% w/v α-gelatin cannot gel by this mechanism, and only form viscous liquids.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformation of β-casein A in the monomeric and thermally aggregated states has been investigated by a range of techniques. β-Casein exists as a monomer in solution at 4°C and at concentrations up to at least 3 g/dl. The molecule is flexible and exhibits a lot of segmental motion, but its secondary structure is not wholly random coil; about one-third of the polypeptide chain is ordered and the likely locations of these regions are discussed. The radius of gyration, representing the time-average distribution of the flexible chain, is 46 Å. Increasing temperature leads to aggregation of the β-casein molecules. The degree of association is very sensitive to experimental conditions, and under our conditions a 14-mer exists at 20°C. The aggregate is spherical with a radius of about 100 Å. The interior of the aggregate is relatively disordered, and the β-casein molecules remain in a largely flexible, hydrated conformation. The volume restriction of the protein molecules which occurs on association leads to some immobilization of the hydrophobic C-terminal region, which is packed toward the center of the aggregate.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A sedimentation analysis has been used to determine the proportion of protein present as monomer and aggregate in 0.5 and 1.0 g/dl solutions of β-casein A in pH 7 phosphate buffer over the temperature range 10-40°C. The amount and molecular weight of the aggregate increase with temperature; under the conditions used, the aggregation number (n) of β-casein is given approximately by n = 0.6t + 2 with t in degrees centigrade. The concentration of β-casein in monomeric and aggregated states at different temperatures is used to calculate the standard enthalpy of aggregation ΔH° (Van't Hoff) by assuming that β-casein undergoes a cooperative, two-state, micellization process; aggregation is an endothermic process and ΔH° = 66.0 ± 2.6 kJ mol-1. Combination of this ΔH° with the amount of protein calculated to dissociate when 1 g/dl solutions are diluted isothermally to 0.5 g/dl gives the heat of dilution at various temperatures. These calculated heats of dilution are compared with the experimental values obtained by carrying out the same dilutions in a microcalorimeter. The heat of dilution decreases linearly with β-casein concentration, but the extrapolated zero-concentration values of 65.8 ± 1.6 kJ mol-1 is the same as the Van't Hoff enthalpy. This agreement in the enthalpy values indicates that the micellization of β-casein occurs cooperatively. The effect of modifying the hydrophobic/hydrophilic balance of the system on the micellization of β-casein A has been investigated. The hydrophobic interaction between the protein molecules is decreased by removing the three C-terminal residues (Ileu Ileu Val) with carboxypeptidase-A. This modification drastically reduces the ability of the β-casein molecule to form micelles. Substitution of 2H2O for H2O at constant temperature perturbs the monomer-micelle equilibrium in favor of micelles because of enhanced hydrophobic interactions in the former solvent. The results are consistent with β-casein micellization involving a delicate balance of the hydrophobic forces favoring aggregation and electrostatic forces opposing it.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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