DOI: 10.1016/j.bbapap.2005.10.012. β-lactoglobulin under high pressure studied by small-angle neutron scattering

β-lactoglobulin under high pressure studied by small-angle neutron scattering

10.1016/j.bbapap.2005.10.012

Crossref journal-article

Elsevier BV

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (78)

Bibliography

Loupiac, C., Bonetti, M., Pin, S., & Calmettes, P. (2006). Î²-lactoglobulin under high pressure studied by small-angle neutron scattering. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1764(2), 211â216.

Authors 4

C. Loupiac (first)
M. Bonetti (additional)
S. Pin (additional)
P. Calmettes (additional)

References 35 Referenced 25

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10.1177/108201329500100203 / Food Sci. Technol. Int. / Review: high pressure, microbial inactivation and food preservation by Cheftel (1995)
10.1016/S0924-2244(97)01015-7 / Trends Food Sci. Technol. / The use of high pressure to modify the functionality of food proteins by Messens (1997)
10.1016/j.tifs.2003.08.005 / Trends Food Sci. Technol. / Advantages of high pressure sterilisation on quality of food products by Matser (2004)
{'key': '10.1016/j.bbapap.2005.10.012_bib6', 'series-title': 'Food Proteins', 'first-page': '51', 'article-title': 'Relationships between structure and functional properties', 'author': 'Kinsella', 'year': '1981'} / Food Proteins / Relationships between structure and functional properties by Kinsella (1981)
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10.1146/annurev.pc.44.100193.000513 / Annu. Rev. Phys. Chem. / Pressure stability of proteins by Silva (1993)
10.1016/S0268-005X(01)00017-0 / Food Hydrocolloids / Effects of high pressure and low temperature on β-lactoglobulin unfolding and aggregation by Kolakowski (2001)
10.1016/S1466-8564(02)00045-0 / Innov. Food Sci. Emerg. Technol. / High pressure as a tool to study some proteins properties: conformational modification, activity and oligomeric dissociation by Lullien-Pellerin (2002)
10.1021/jf970652f / J. Agric. Food Chem. / Gel formation from industrial milk whey proteins under hydrostatic pressure: effect of hydrostatic pressure and protein concentration by Kanno (1998)
10.1006/jmbi.2000.4350 / J. Mol. Biol. / High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulin by Kuwata (2001)
10.1016/S0968-0004(01)01949-1 / Trends Biochem. Sci. / Pressure provides new insights into protein folding, dynamics and structure by Silva (2001)
{'key': '10.1016/j.bbapap.2005.10.012_bib14', 'series-title': 'High pressure bioscience and biotechnology', 'first-page': '117', 'article-title': 'Pressure induced molten globule states of proteins', 'volume': 'vol. 13', 'author': 'Masson', 'year': '1996'} / High pressure bioscience and biotechnology / Pressure induced molten globule states of proteins by Masson (1996)
10.1046/j.1432-1033.2002.03126.x / Eur. J. Biochem. / High pressure effects on horse heart metmyoglobin studied by small-angle neutron scattering by Loupiac (2002)
10.1017/S0022029900021713 / J. Dairy Res. / A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160 °C by De Wit (1981)
10.1016/0301-4622(89)80053-5 / Biophys. Chem. / Calorimetric and circular dichroic studies of the thermal denaturation of β-lactoglobulin by Lapange (1989)
10.1016/S0141-8130(97)00089-5 / Int. J. Biol. Macromol. / Reversibility of heat induced conformational changes and surface exposed hydrophobic clusters of β-lactoglobulin: their role in heat-induced sol–gel transition by Relkin (1998)
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10.1051/jcp/1996930987 / J. Chim. Phys. / Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH7 by Aymard (1996)
10.1046/j.1365-2621.1999.00311.x / Int. J. Food Sci. Technol. / Structural and interaction properties of β-lactoglobulin as studied by FTIR spectroscopy by Lefèvre (1999)
10.1042/bj3240341 / Biochem. J. / effect of temperature on the secondary structure of the β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: test of the molten globule hypothesis by Qi (1997)
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10.1021/jf960383d / J. Agric. Food Chem. / High pressure promotes β-lactoglobulin aggregation through SH/S–S interchange reactions by Funtenberger (1997)
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10.1021/bi982825f / Biochemistry / Differences between the pressure and temperature induced denaturation and aggregation of β-lactoglobulin A, B and AB monitored by FT-IR spectroscopy and small-angle X ray scattering by Panick (1999)
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Dates

Type	When
Created	19 years, 9 months ago (Nov. 8, 2005, 2:14 a.m.)
Deposited	6 years, 4 months ago (April 4, 2019, 4:18 a.m.)
Indexed	1 week, 2 days ago (Aug. 21, 2025, 12:37 p.m.)
Issued	19 years, 6 months ago (Feb. 1, 2006)
Published	19 years, 6 months ago (Feb. 1, 2006)
Published Print	19 years, 6 months ago (Feb. 1, 2006)

Funders 0

None

BibTeX

@article{Loupiac_2006, title={β-lactoglobulin under high pressure studied by small-angle neutron scattering}, volume={1764}, ISSN={1570-9639}, url={http://dx.doi.org/10.1016/j.bbapap.2005.10.012}, DOI={10.1016/j.bbapap.2005.10.012}, number={2}, journal={Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics}, publisher={Elsevier BV}, author={Loupiac, C. and Bonetti, M. and Pin, S. and Calmettes, P.}, year={2006}, month=feb, pages={211–216} }

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