title: Interaction between Vaccinium bracteatum Thunb. leaf pigment and rice proteins.
abstract: In this study, we investigated the interaction of Vaccinium bracteatum Thunb. leaf (VBTL) pigment and rice proteins. In the presence of rice protein, VBTL pigment antioxidant activity and free polyphenol content decreased by 67.19% and 68.11%, respectively, and L(∗) of the protein-pigment complex decreased significantly over time. L(∗) values of albumin, globulin and glutelin during 60-min pigment exposure decreased by 55.00, 57.14, and 54.30%, respectively, indicating that these proteins had bound to the pigment. A significant difference in protein surface hydrophobicity was observed between rice proteins and pigment-protein complexes, indicating that hydrophobic interaction is a major binding mechanism between VBTL pigment and rice proteins. A significant difference in secondary structures between proteins and protein-pigment complexes was also uncovered, indicating that hydrogen bonding may be another mode of interaction between VBTL pigment and rice proteins. Our results indicate that VBTL pigment can stain rice proteins with hydrophobic and hydrogen interactions.
authors.affiliation: State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
authors.forename: Li
authors.initials: L
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
authors.forename: Yuan
authors.initials: Y
authors.lastname: Xu
authors.affiliation: Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
authors.forename: Sumei
authors.initials: S
authors.lastname: Zhou
authors.affiliation: State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China. Electronic address: qianhaifeng@jiangnan.edu.cn.
authors.forename: Haifeng
authors.initials: H
authors.lastname: Qian
authors.affiliation: State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
authors.forename: Hui
authors.initials: H
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
authors.forename: Xiguang
authors.initials: X
authors.lastname: Qi
authors.affiliation: Jiangsu Institute of Poultry Sciences, Yangzhou 225125, China.
authors.forename: Meihua
authors.initials: M
authors.lastname: Fan
mesh_terms: D000418:Albumins / Q000737:chemistry; D004347:Drug Interactions; D005916:Globulins / Q000737:chemistry; D005983:Glutens / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D012275:Oryza / Q000737:chemistry*; D010860:Pigments, Biological / Q000737:chemistry*; D010936:Plant Extracts / Q000737:chemistry; D018515:Plant Leaves / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D029796:Vaccinium / Q000737:chemistry*
chemical_list: D000418:Albumins; D005916:Globulins; D010860:Pigments, Biological; D010936:Plant Extracts; D010940:Plant Proteins; D005983:Glutens
keywords: Hydrogen bonding; Hydrophobic interaction; Rice protein; Secondary structure; Surface hydrophobicity; Vaccinium bracteatum Thunb.