Two-step complex behavior between Bowman-Birk protease inhibitor and ι-carrageenan: Effect of protein concentration, ionic strength and temperature
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- 作者：Xingfei Li ; Yufei Hua ; yfhua@jiangnan.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Yeming Chen ; Xiangzhen Kong ; Caimeng Zhang
- 关键词：Complex coacervation ; Bowman&ndash ; Birk protease inhibitor ; ι-Carrageenan ; Hydrophobic interactions ; Isothermal titration calorimetry
- 刊名：Food Hydrocolloids
- 出版年：2017
- 出版时间：January 2017
- 年：2017
- 卷：62
- 期：Complete
- 页码：1-9
- 全文大小：708 K
文摘
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At high ionic strength, pHc occurred at the pH lower than isoelectric point of BBI.
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The binding of BBI to ι-carrageenan formed a two-step binding.
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The presence of nonelectrostatic interactions at the first binding step was proved.
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rcritical was independent of protein concentration, ionic strength and temperature.