Carbodiimide stabilizes the ultrasound-pretreated camelina protein structure with improved water resistance

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• 作者：Xiangwei Zhu^a ; Donghai Wang^b ; Xiuzhi Susan Sun^a ; ^xss@ksu.edu
• 关键词：DCM ; defatted camelina meal ; CP ; camelina protein ; CPI ; camelina protein isolate ; UCPI ; ultrasound-modified camelina protein isolate ; EDC ; ethyl-3-(3-dimethyl-aminopropyl-1-carbodiimide) ; NHS ; N-hydroxysuccinimide
• 刊名：Industrial Crops and Products
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：97
• 期：Complete
• 页码：196-200
• 全文大小：1019 K
• 卷排序：97

文摘

EDC-induced crosslink reaction stabilized camelina protein’s structures. The newly-formed amide bond stimulated protein’s intermolecular interaction. The stabilized camelina protein structure became more rigid and water resistant. Ultrasound unfolding pretreatment increased protein’s crosslink degree. Molecular characteristics of cross-linked camelina protein were discussed.