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Article: Molecular and Microstructural Studies of Thermal Denaturation and Gelation of β-Lactoglobulins A and B
Title | Molecular and Microstructural Studies of Thermal Denaturation and Gelation of β-Lactoglobulins A and B |
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Authors | |
Keywords | Β-Lactoglobulin Denaturation Differential Scanning Calorimetry Electron Microscopy Gelation Genetic Variants Infrared Spectroscopy |
Issue Date | 1997 |
Publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau |
Citation | Journal Of Agricultural And Food Chemistry, 1997, v. 45 n. 5, p. 1608-1618 How to Cite? |
Abstract | The thermal properties of β-lactoglobulins (β-lg) A and B at pH 3, 5, 7, and 8.6 were studied by differential scanning calorimetry. Fourier transform infrared spectroscopy was used to monitor changes in the secondary structure of the proteins when heated from 25 to 95 °C. The microstracture of β-lg A and B gels made from 10% (w/v) protein solutions by heating at 90 °C for 30 min was studied by scanning and transmission electron microscopy. β-Lg B had greater thermal stability and required more energy to denature than β-lg A; denaturation of β-lg B was also more cooperative. Infrared spectroscopy showed that β-lg B had a higher proportion of β-sheet than the A variant at pH 3 and 5. At pH 7 and 8.6 the secondary structures of the two variants were similar. At all four pH values, aggregation bands (1682 and ∼1622 cm -1) were observed when the proteins were heated. Electron microscopy showed that the gel matrix of β-lg B at both acid and alkaline pH was made up of larger aggregate structures than β-lg A. The aggregates formed by both variants were large (1-2 μm) and globular at acid pH but much smaller (nanometer range) and amorphous at alkaline pH. This information provides a useful model for studying the relationship between protein structure and function. |
Persistent Identifier | http://hdl.handle.net/10722/178843 |
ISSN | 2023 Impact Factor: 5.7 2023 SCImago Journal Rankings: 1.114 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Boye, JI | en_US |
dc.contributor.author | Ma, CY | en_US |
dc.contributor.author | Ismail, A | en_US |
dc.contributor.author | Harwalkar, VR | en_US |
dc.contributor.author | Kalab, M | en_US |
dc.date.accessioned | 2012-12-19T09:50:05Z | - |
dc.date.available | 2012-12-19T09:50:05Z | - |
dc.date.issued | 1997 | en_US |
dc.identifier.citation | Journal Of Agricultural And Food Chemistry, 1997, v. 45 n. 5, p. 1608-1618 | en_US |
dc.identifier.issn | 0021-8561 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178843 | - |
dc.description.abstract | The thermal properties of β-lactoglobulins (β-lg) A and B at pH 3, 5, 7, and 8.6 were studied by differential scanning calorimetry. Fourier transform infrared spectroscopy was used to monitor changes in the secondary structure of the proteins when heated from 25 to 95 °C. The microstracture of β-lg A and B gels made from 10% (w/v) protein solutions by heating at 90 °C for 30 min was studied by scanning and transmission electron microscopy. β-Lg B had greater thermal stability and required more energy to denature than β-lg A; denaturation of β-lg B was also more cooperative. Infrared spectroscopy showed that β-lg B had a higher proportion of β-sheet than the A variant at pH 3 and 5. At pH 7 and 8.6 the secondary structures of the two variants were similar. At all four pH values, aggregation bands (1682 and ∼1622 cm -1) were observed when the proteins were heated. Electron microscopy showed that the gel matrix of β-lg B at both acid and alkaline pH was made up of larger aggregate structures than β-lg A. The aggregates formed by both variants were large (1-2 μm) and globular at acid pH but much smaller (nanometer range) and amorphous at alkaline pH. This information provides a useful model for studying the relationship between protein structure and function. | en_US |
dc.language | eng | en_US |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau | en_US |
dc.relation.ispartof | Journal of Agricultural and Food Chemistry | en_US |
dc.subject | Β-Lactoglobulin | en_US |
dc.subject | Denaturation | en_US |
dc.subject | Differential Scanning Calorimetry | en_US |
dc.subject | Electron Microscopy | en_US |
dc.subject | Gelation | en_US |
dc.subject | Genetic Variants | en_US |
dc.subject | Infrared Spectroscopy | en_US |
dc.title | Molecular and Microstructural Studies of Thermal Denaturation and Gelation of β-Lactoglobulins A and B | en_US |
dc.type | Article | en_US |
dc.identifier.email | Ma, CY: macy@hkucc.hku.hk | en_US |
dc.identifier.authority | Ma, CY=rp00759 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.scopus | eid_2-s2.0-0642302370 | en_US |
dc.identifier.hkuros | 35926 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0642302370&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 45 | en_US |
dc.identifier.issue | 5 | en_US |
dc.identifier.spage | 1608 | en_US |
dc.identifier.epage | 1618 | en_US |
dc.identifier.isi | WOS:A1997XA02800015 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Boye, JI=7003390065 | en_US |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_US |
dc.identifier.scopusauthorid | Ismail, A=7201548364 | en_US |
dc.identifier.scopusauthorid | Harwalkar, VR=35605979700 | en_US |
dc.identifier.scopusauthorid | Kalab, M=7005921318 | en_US |
dc.identifier.issnl | 0021-8561 | - |