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This study focused on elucidating the non-covalent interactions between hemp seed globulin (GLB) and two hemp seed phenolic compounds, Cannabisin A (CA) and Cannabisin B (CB), and to explore these interactions on the protein's structure, conformation, and functionality. Fluorescence quenching and thermodynamic analysis revealed that static quenching governed non-covalent interaction processes, with hydrogen bonds and van der Waals forces functioning as major forces. This was further substantiated by molecular docking studies. The binding affinity order was CA > CB, indicating that the specific phenolic compound had a notable impact on the binding affinity. Furthermore, when complexed with CA, Tyr and Trp residues were exposed to a more hydrophilic environment than when complexed with CB. It was noted that the complexation with either CA or CB consistently affects GLB's secondary structure, particle size, and ζ-potential. GLB treated with the phenolic compounds exhibited enhanced ABTS and DPPH scavenging activities and improved digestibility compared to untreated GLB. Furthermore, the non-covalent interactions significantly increased CA's water solubility, highlighting GLB as a promising natural carrier for hydrophobic bioactive components. These findings hold potential implications for enhancing hemp seed protein applications within the food industry by positively influencing its functional properties and bioactivity., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. No conflict of interest exists in the submission of this manuscript, and the manuscript is approved by all authors for publication., (Copyright © 2023 Elsevier B.V. All rights reserved.)

This study develops hemp seed globulin (GLB)-alginate (ALG) nanoparticles (GANPs) for Cannabisin A (CA) stabilization under environmental stress and during pepsin digestion. The optimal GLB: ALG mass ratio of 1: 1.5 was determined for GANPs formation at pH 3.5, resulting in a high yield of 95.13 ± 0.91 %, a ζ-potential of -35.73 ± 1.04 mV, a hydrodynamic diameter of 470.67 ± 11.36 nm, and a PDI of 0.298 ± 0.016. GANPs were employed to encapsulate CA, achieving a high loading capacity of 13.48 ± 0.04 μg mg -1 . FTIR analysis demonstrated that the formation of CA-GLB-ALG nanoparticles (CGANPs) involves electrostatic interactions, hydrogen bonding, and hydrophobic interactions. XRD and DSC analyses revealed that CA is amorphous within the CGANPs. CGANPs demonstrated remarkable dispersion stability as well as resistance to high ionic strength and high-temperature treatments, indicating their potential as efficient hydrophobic drug-delivery vehicles. When compared to free CA, CA coated within CGANPs displayed greater DPPH/ABTS scavenging activity. Furthermore, the ALG-shelled nanoparticles protected GLB from pepsin digestion and slowed the release of CA throughout the release process, extending their stay on the intestinal wall mucosa. These findings imply that CGANPs is an ideal delivery vehicle for CA as they may expand the application of CA in food items., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023. Published by Elsevier B.V.)