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µÚһƪÌâÄ¿Ãû×ÖÊÇEffect of heat treatment on the antigenicity of bovine -lactalbumin and -lactoglobulin in whey protein isolate
×÷Õß: Bu GH (Bu, Guanhao)1, Luo YK (Luo, Yongkang)1, Zheng Z (Zheng, Zhe)1, Zheng H (Zheng, Hai)1 À´Ô´³ö°æÎï: FOOD AND AGRICULTURAL IMMUNOLOGY    ¾í: 20    ÆÚ: 3    Ò³: 195-206    ³ö°æÄê: 2009   

µÚ¶þƪÊÇMolecular modifications of beta-lactoglobulin upon exposure to high pressure
×÷Õß: Iametti S, Transidico P, Bonomi F, Vecchio G, Pittia P, Rovere P, DallAglio G

À´Ô´³ö°æÎï: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY    ¾í: 45    ÆÚ: 1    Ò³: 23-29    ³ö°æÄê: JAN 1997   

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[ Last edited by zhongjunzhen on 2009-11-12 at 16:31 ]
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Irreversible modifications in tertiary structure, surface hydrophobicity and association state of beta-lactoglobulin were studied after exposure to high pressure (600 and 900 MPa for 5-20 and 1-10 min respectively) of solutions of the protein at neutral pH (pH 6.8) and at concentrations of 2.5, 5 and 10 mg/ml. Only minor irreversible structural modifications were evident even for treatments as intense as 15 min at 900 MPa. The occurrence of irreversible modifications was time-progressive at 600MPabut was complete within 2 min at 900 MPa. The irreversibly-modified protein was soluble, but some covalent aggregates were formed. Formation of aggregates increased with increasing protein concentration and was prevented by blocking the free thiolmoiety in each beta-lactoglobulin monomer. Results are discussed in the light of their practical relevance, and a unifying denaturation mechanism is proposed for beta-lactoglobulin. In the proposed mechanism, release of monomers represents one of the earliestevents, while association of transiently modified monomers stabilizes the denatured forms of the protein.
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