Cold plasma (CP) treatment was used to prepare the glycosylation conjugates of high-temperature peanut protein isolate (HPPI) and lactose to improve the solubility of HPPI. We observed that by increasing the CP treatment time to 3 min, the solubility of the conjugates increased to 1.34 mg/mL. An increase in the degree of glycosylation and a decrease in the degree of browning indicated that although CP treatment accelerated the glycosylation of HPPI and lactose, it interfered with the formation of melanoidin. The analysis of protein tertiary structure showed that tryptophan and tyrosine residues in proteins undergoing CP treatment were the primary sites for the Maillard reaction. The relative decrease in surface hydrophobicity and FT-IR analysis indicated that the increase in the -OH stretching vibration intensity on the protein surface represented the formation of the covalent bonds between HPPI and lactose during the CP treatment. An increase in the denaturation temperature of proteins was observed after grafting with lactose. Changes in the secondary structure and surface structure of proteins showed that lactose covalently bonded to the surface of HPPI during CP treatment, forming a more stable ordered structure.
Keywords: Cold plasma treatment; Lactose; Peanut protein.
Copyright © 2018. Published by Elsevier B.V.