Buenos Aires and Kyoto targets do little to reduce climate change impacts
Buenos Aires and Kyoto targets do little to reduce climate change impacts
Sodium caseinate hydrolysates were generated at laboratory-scale using 28 commercial protease preparations of bacterial, fungal, plant and animal origin. Caseinophosphopeptides (CPPs) were enriched from these hydrolysates by calcium chloride aggregation at pH 7.5 followed by ethanol precipitation of the aggregates. CPP yield ranged from 3.4 to 16.0% (w/w) of the original protein. The calcium binding and solubilising abilities of the enriched CPPs ranged from 0.40 to 0.61 and 7.4 to 24.0mg Ca2+mg-1CPP, respectively. Hydrolysis of sodium caseinate with Bioprotease N100L resulted in a 16.0% yield of CPPs which could solubilise 19.1mgCa2+mg-1 CPP. Significant differences in the gel permeation and reversed-phase chromatography profiles for the various enriched CPPs were evident. In general, no apparent relationship was observed between hydrolysate degree of hydrolysis (DH%), CPP yield, CPP calcium binding and solubilising abilities, and CPP apparent molecular mass distribution and hydrophobic peptide profiles
285-289
McDonagh, D.
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FitzGerald, R.J.
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Parry, M
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Arnell, N.W.
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Hulme, M.
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Nicholls, R.J.
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Livermore, M.
9912800a-9ba8-4acf-9a7e-cc9a199709a3
November 1998
McDonagh, D.
b57d01ec-6612-4a12-ab92-5cb679fdbc94
FitzGerald, R.J.
08610be2-8ee8-4af6-8dd6-b175b9602ad0
Parry, M
186384dc-1aa9-4744-b4fa-eb7e59113659
Arnell, N.W.
196119de-cdf5-4ba8-a5d5-5e5cf4c88085
Hulme, M.
b65e2b3d-f0ef-4ba9-8dde-e29d9c966b7a
Nicholls, R.J.
4ce1e355-cc5d-4702-8124-820932c57076
Livermore, M.
9912800a-9ba8-4acf-9a7e-cc9a199709a3
McDonagh, D., FitzGerald, R.J., Parry, M, Arnell, N.W., Hulme, M., Nicholls, R.J. and Livermore, M.
(1998)
Buenos Aires and Kyoto targets do little to reduce climate change impacts.
Global Environmental Change, 8 (4), .
(doi:10.1016/S0959-3780(98)00019-3).
Abstract
Sodium caseinate hydrolysates were generated at laboratory-scale using 28 commercial protease preparations of bacterial, fungal, plant and animal origin. Caseinophosphopeptides (CPPs) were enriched from these hydrolysates by calcium chloride aggregation at pH 7.5 followed by ethanol precipitation of the aggregates. CPP yield ranged from 3.4 to 16.0% (w/w) of the original protein. The calcium binding and solubilising abilities of the enriched CPPs ranged from 0.40 to 0.61 and 7.4 to 24.0mg Ca2+mg-1CPP, respectively. Hydrolysis of sodium caseinate with Bioprotease N100L resulted in a 16.0% yield of CPPs which could solubilise 19.1mgCa2+mg-1 CPP. Significant differences in the gel permeation and reversed-phase chromatography profiles for the various enriched CPPs were evident. In general, no apparent relationship was observed between hydrolysate degree of hydrolysis (DH%), CPP yield, CPP calcium binding and solubilising abilities, and CPP apparent molecular mass distribution and hydrophobic peptide profiles
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Published date: November 1998
Organisations:
Energy & Climate Change Group
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Local EPrints ID: 350862
URI: http://eprints.soton.ac.uk/id/eprint/350862
ISSN: 0959-3780
PURE UUID: 18a5b3b1-8184-4253-88b9-2add02049e1f
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Date deposited: 12 Apr 2013 10:43
Last modified: 15 Mar 2024 03:18
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Author:
D. McDonagh
Author:
R.J. FitzGerald
Author:
M Parry
Author:
N.W. Arnell
Author:
M. Hulme
Author:
M. Livermore
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