Mechanisms underlying the complexation of zein fibrils via plasma assisted acid-heat (AH) treatment with gum Arabic (GA): Enhanced emulsification performance

Yaxiao Wang; Siqi Han; Yuru Feng; Xiaojun Xue; Mingrui Fu; Peng Guo; Shuang Dong

doi:10.1016/j.ijbiomac.2025.145080

Mechanisms underlying the complexation of zein fibrils via plasma assisted acid-heat (AH) treatment with gum Arabic (GA): Enhanced emulsification performance

Int J Biol Macromol. 2025 Jun 25:145080. doi: 10.1016/j.ijbiomac.2025.145080. Online ahead of print.

Authors

Yaxiao Wang¹, Siqi Han¹, Yuru Feng¹, Xiaojun Xue¹, Mingrui Fu¹, Peng Guo², Shuang Dong³

Affiliations

¹ School of Agricultural Engineering and Food Science, Shandong University of Technology, Zibo 255000, PR China.
² School of Agricultural Engineering and Food Science, Shandong University of Technology, Zibo 255000, PR China; Shandong Laboratory of Advanced Materials and Green Manufacturing, Yantai 265503, PR China. Electronic address: gpeng@sdut.edu.cn.
³ School of Agricultural Engineering and Food Science, Shandong University of Technology, Zibo 255000, PR China; Shandong Bailong Chuangyuan Bio-tech Co., Ltd, Dezhou 251200, PR China. Electronic address: dongshuangsdut@126.com.

PMID: 40578644
DOI: 10.1016/j.ijbiomac.2025.145080

Abstract

Cold plasma was applied in the present work as an assistant technology for acid-heat (AH) treatment to prepare zein fibrils (PZF) and the binary complex of PZF and gum Arabic (GA) was fabricated through electrostatic combination method. The results indicated that the particle size of PZF-G complex was increased significantly. Zeta-potential was dramatically changed from positive charge of 33.1 ± 1.0 mV (PZF) to negative charge (-18.5 ± 0.2 mV of PZF-G_10:1) after incorporated with GA. Micromorphology showed that PZF was wrapped by GA and formed a smooth and flat membrane structure at PZF-G complex mass ratio of 3:1. The blue-shift occurred around 3294.9 cm^-1 in FTIR spectrum suggested that more hydrogen bonds were formed and a transformation from α-helix to β-sheet was observed within complex. The higher proportion of GA promoted more disulfide bonds generated in PZF molecules, which further reinforced the structural strength of the complex. PZF-G complex exhibited higher emulsifying activity and better long-term storage stability, especially for PZF-G_3:1. The high molecular flexibility of PZF would provide more binding sites for complexing with GA and the complex exhibited better performance. Findings from this study would bring a new insight into the development of protein-based Pickering emulsion with high performance stability.

Keywords: Binary complex; Cold plasma; Fibrils; Gum arabic; Pickering emulsion; Zein.