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

Published Date
Industrial Crops and Products
March 2017, Vol.97:196–200, doi:10.1016/j.indcrop.2016.11.001
Short communication

Author 

• Xiangwei Zhu ^a
• Donghai Wang ^b
• Xiuzhi Susan Sun ^a,,

• aBio-Materials and Technology Laboratory, Department of Grain Science and Industry Kansas State University, Manhattan, KS 66506, United States
• bDepartment of Biological and Agricultural Engineering, Kansas State University, Manhattan, KS 66506, United States

Received 19 August 2016. Revised 5 October 2016. Accepted 1 November 2016. Available online 22 December 2016. 

Highlights

• •
  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.

Abstract

Camelina protein showed poor water resistance, which restrained its industrial application, such as for adhesives or coatings. In this research, the effect of ultrasound pretreatment and carbodiimide coupling on water resistance of camelina protein isolate (CPI) was discussed. Camelina protein was extracted from defatted camelina meal by alkali solubilization and acid precipitation and treated by high intensity ultrasound. Both CPI and ultrasound-modified CPI (UCPI) were cross-linked by Ethyl-3-(3-dimethyl-aminopropyl-1-carbodiimide) (EDC). The cross-linked CPI exhibited increased molecular weight and particle size due to the amide bond formation between free amino groups and carboxyl groups. Accordingly, microstructures of the coupled protein became rigid and condensed with increased aqueous stability. The crosslink degree of UCPI was higher than CPI, leading to UCPI’s better water resistance, more compact microstructures and larger particle size.

Graphical abstract

Abbreviations

• 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

Keywords

• Camelina protein
• Crosslink
• EDC
• Ultrasound treatment
• Intermolecular protein interaction
• Water resistance

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• DOC (604K)

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  Corresponding author.

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