pH-Induced Structural Transitions during Complexation and Coacervation of â-Lactoglobulin and Acacia Gum (Record no. 44981)

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control field 20250625140637.0
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Transcribing agency CICY
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Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-10749
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Title pH-Induced Structural Transitions during Complexation and Coacervation of â-Lactoglobulin and Acacia Gum
490 0# - SERIES STATEMENT
Volume/sequential designation Langmuir, 21, p.386-394, 2005
520 3# - SUMMARY, ETC.
Summary, etc. pH-induced structural changes during complex coacervation between â-lactoglobulin (BLG)and Acacia gum (AG)in aqueous solutions were determined by coupling slow in situ acidification of BLG/AG mixed dispersions and different experimental methods. The combined signal evolution of dynamic light scattering at 90° scattering angle (I90), electrophoretic mobility, turbidimetry (ô), circular dichroism, and phase contrast microscopy allowed the distinction of critical structural transitions and the definition of their corresponding pH. The formation of soluble BLG/AG complexes was initiated at pHsc (4.90), since I90 and ô significantly increased from the baseline. In parallel or just following complexation, a conformational change of BLG was detected at pHpct (4.8). An increase in positive charge density of BLG induced complex aggregation atpHca (4.7). More efficient charge neutralization of aggregated complexes, especially through the lowering of thenumberofAGnegative charges, promoted initiation of phase separation atpHpsi (4.4).Mixeddispersions became unstable and phase separation occurred at pHps (4.2). The phase separation of mixed dispersions was suggested by the maximum value of scattered light, by an important acceleration of the dispersion turbidity, by a strong increase of hydrod dynamic radii, and by the first appearance of light fluctuations as observed by phase contrast microscopy. At the microscopic level, the first coacervates were observed at pHcoa (4.0), near the pH of the maximum of turbidity. It was also noticed that, from the onset of interactions between biopolymers, the pH decrease led to (i)a gradual homogenization of particle size in the mixed dispersion as suggested by the decrease of dispersion polydispersity and (ii)conformational transitions of the protein (a loss of R-helix structure at pHpct and a gain in protein secondary structure near pHcoa, probably involving â-sheet components).
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Mekhloufi, G.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Sanchez, C.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Renard, D.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Guillemin, S.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Hardy, J.
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Uniform Resource Identifier <a href="https://drive.google.com/file/d/1hopxRUScVm582N_ZXhKpCB_7wtJfvpcs/view?usp=drivesdk">https://drive.google.com/file/d/1hopxRUScVm582N_ZXhKpCB_7wtJfvpcs/view?usp=drivesdk</a>
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-10749 25.06.2025 25.06.2025 Documentos solicitados