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Çë´ó¼Ò°ïæÕÒÁ½ÆªÎÄÏ×£º 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 ÐèҪȫÎÄ£¬Èç¹ûÄÜÕÒµ½Çë·¢µ½ÎÒµÄÓÊÏäzhongjunzhen@163.com,·Ç³£¸Ðл~~ ![]() [ 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. ÎÒÕÒÕÒ Î´±ØÓÐ |
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