文献类型：期刊文献

英文题名：Enhancing oil-water interfacial behavior and emulsion properties of abalone protein hydrolysate-inulin conjugates by pH-shift pretreatment and Maillard reaction

作者：Li, Jinzhen[1,2];Cao, Wenhong[1,2];Lin, Haisheng[1,2];Gao, Jialong[1,2];Chen, Zhongqin[1,2];Zheng, Huina[1,2,3]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Natl Res & Dev Branch Ctr Shellfish Proc Zhanjiang, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China;[2]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518120, Peoples R China;[3]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Guangdong, Peoples R China

年份：2027

卷号：185

外文期刊名：FOOD HYDROCOLLOIDS

收录：SCI-EXPANDED(收录号：WOS:001898142300002)、、WOS

基金：This work was supported by the National Key Research and Devel-opment Program of China (2024YFD2401805) , the Shellfish & Algae Industry Innovation Team of Guangdong Modern Agricultural Tech-nology System (2024CXTD23) , the Guangdong Basic and Applied Basic Research Foundation (2024A1515010955) , and the Modern Agricul-tural Industry Technology Research System of China (CARS-49) .

语种：英文

外文关键词：Abalone protein hydrolysate; Inulin; pH-shift; Maillard reaction; Interfacial behavior

外文摘要：Abalone protein hydrolysate (APH) has potential as a marine-derived food protein ingredient, but its limited ability to form mechanically stable oil-water interfacial films restricts its application in emulsion systems. In this study, APH and inulin were subjected to Maillard reaction under neutral wet-heating or alkaline pH-shift-assisted conditions to determine how pH-dependent structural regulation influences interfacial behavior and emulsion properties. Compared with neutral wet-heating, alkaline treatment suppressed heat-induced aggregation, increased conformational flexibility, and induced rearrangement of the secondary structure of APH. Subsequent covalent conjugation with inulin further modified surface wettability and electrostatic interactions, producing a more dispersed conjugate with improved hydrophilic-hydrophobic balance. These structural and colloidal changes facilitated interfacial penetration and molecular rearrangement, and promoted the formation of a stronger and more deformation-resistant interfacial film. Consequently, emulsions stabilized by the alkalinetreated APH-inulin conjugate exhibited a narrower droplet size distribution, and more pronounced shearthinning behavior. In contrast, neutral wet-heating favored aggregate formation and limited effective interfacial organization. These findings indicate that alkaline pH modulation not only facilitates APH-inulin conjugation but also regulates the competition between heat-induced aggregation and glycation-associated interfacial assembly, providing a mechanistic basis for improving the functionality of marine protein hydrolysates in food emulsion systems.