Thermal Properties of Yak α-Lactalbumin and β-Lactoglobulin: a DSC Study

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dc.contributor.authorWang, Lifeng
dc.contributor.authorMa, Ying
dc.contributor.authorCui, Jie
dc.contributor.authorOyeyinka, Samson
dc.contributor.authorHe, S
dc.contributor.authorLi, He
dc.date.accessioned2018-06-05T08:18:45Z
dc.date.available2018-06-05T08:18:45Z
dc.date.issued2017-09-18
dc.description.abstractA differential scanning calorimetry (DSC) method was used to investigate the denaturation temperature of yak α-lactalbumin (α-La), β-lactoglobulin (β-Lg), and a mixture of two proteins and the thermal properties of α-La and β-Lg in the presence of glucose, lactose, sucrose, NaCl, CaCl2, and at various pH (4.0–10.0). The denaturation temperature (T d) of α-La increased from 52.1 °C in the absence of β-Lg to 53.9 °C in the presence of β-Lg, while the T d of β-Lg decreased from 81.4 °C in the absence of α-La to 79.9 °C in the presence of α-La. α-La was thermal stable in the range of pH 4.0–10.0, while β-Lg was more thermal stable in acidic pH than in alkaline pH. Sugars, Na+, and Ca2+ influenced the stabilization of the two proteins against thermal denaturation with greatly influenced for β-Lg. α-La kept reversibility in the presence of sugars, NaCl, CaCl2, and over a wide pH range (4.0–10.0), with most of the reversibility values being greater than 90%. In contrast, β-Lg was completely irreversible whether in its native state or in the presence of the additives.en_US
dc.identifier.urihttp://hdl.handle.net/123456789/356
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.subjectYak milken_US
dc.subjectα-Lactalbuminen_US
dc.subjectβ-Lactoglobulinen_US
dc.subjectDSC differential scanning calorimetryen_US
dc.subjectThermal denaturationen_US
dc.titleThermal Properties of Yak α-Lactalbumin and β-Lactoglobulin: a DSC Studyen_US
dc.typeArticleen_US

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