Caseinomacropeptide modifies the heat-induced denaturation-aggregation process of 尾-lactoglobulin

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• 作者：Thomas Croguennec^a ; ^b ; ^c ; ^{Thomas.croguennec@agrocampus-ouest.fr" class="auth_mail} ; Ning Leng^a ; ^b ; ^c ; Pascaline Hamon^a ; ^b ; Florence Rousseau^a ; ^b ; Romain Jeantet^a ; ^b ; ^c ; Saï ; d Bouhallab^a ; ^b
• 刊名：International Dairy Journal
• 出版年：May, 2014
• 年：2014
• 卷：36
• 期：1
• 页码：55-64
• 全文大小：1753 K

文摘

The effect of caseinomacropeptide (CMP) concentration on the kinetics of denaturation of 尾-lactoglobulin (尾-Lg) and on the size and structure of the heat-induced aggregates was investigated over a wide range of pH (3.0-6.7) and temperature (65-95聽掳C). Irrespective of pH and heating temperature, CMP increased the rate of 尾-Lg denaturation. When 尾-Lg and CMP were negatively charged (i.e., at pH 6.7), increasing CMP concentration hindered aggregate formation; the aggregates had a smaller hydrodynamic diameter and the protein solution turbidity decreased. However, when 尾-Lg and CMP were oppositely charged (i.e., at pH 4.0), CMP promoted aggregate formation and large particles (>5聽渭m) were formed on heating. Nevertheless, the covalent aggregates constituting these large particles were of smaller size than those formed on heating 尾-Lg in the absence of CMP. At pH 4.0, CMP induced the formation of large particles when added in a solution of preformed aggregates of 尾-Lg.