Location: Grain Quality and Structure Research
Title: Camelina protein enhanced by polyelectrolyte interaction and its plywood bonding propertiesAuthor
LIU, HAIJING - Kansas State University | |
Bean, Scott | |
SUN, XIUZHI SUSAN - Kansas State University |
Submitted to: Industrial Crops and Products
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 7/26/2018 Publication Date: 8/10/2018 Citation: Liu, H., Bean, S.R., Sun, X. 2018. Camelina protein enhanced by polyelectrolyte interaction and its plywood bonding properties. Industrial Crops and Products. 124:343-352. https://doi.org/10.1016/j.indcrop.2018.07.068. DOI: https://doi.org/10.1016/j.indcrop.2018.07.068 Interpretive Summary: Camelina protein is a major by-product created after oil extraction from camelina seeds; it has drawn research attention as an economical material for bio-industrial implications. The present study investigates the influence of polyelectrolyte interaction on camelina protein structure and effects on wood bonding performance when used as a bio-adhesive. Modification of camelina protein greatly improved both dry and wet adhesion strength when used as an adhesive. Two aliphatic structures with hydrophobic chains were introduced into the chemically modified protein system to further improve the water resistance. This research provides information on how modification of plant proteins can improve their use in bio-materials and can help direct research to improve the use of other plant proteins for such uses. Technical Abstract: Camelina protein is a major by-product created after oil extraction from camelina seeds; it has drawn research attention as an economical material for bio-industrial implications. The present study investigates the influence of polyelectrolyte interaction on camelina protein structure and effects on wood bonding performance when used as a bio-adhesive. Infrared spectroscopy (IR) and transmission electron microscopy (TEM) images revealed that after interacting with polymeric amine epichlorohydrine (PAE), a cationic polyelectrolyte, camelina protein is partly unfolded with more flexible chain structures. PAE works as a bridge among different protein molecules primarily through electrostatic and hydrophobic interactions. Separation by size exclusion chromatography showed that soluble PAE modified proteins are smaller in molecular size. Polymeric amine epichlorohydrine modified proteins had reduced solubility, possibly indicating increased hydrophobicity. The PAE treatment of camelina protein greatly improved both dry and wet adhesion strength when used as an adhesive. Two aliphatic structures with hydrophobic chains were introduced into the PAE modified protein system to further improve the water resistance. This study demonstrates the possibility of camelina as a green resource for the adhesive industry. |