文献类型：期刊文献

英文题名：Functional, structural, and physicochemical properties of spray-dried abalone (Haliotis discus subsp. hannai Ino) protein and hydrolysates with varying degrees of hydrolysis

作者：Zhu, Xiaotong[1];Li, Guiyang[1];Chen, Zhongqin[1,2];Cao, Wenhong[1,2];Lin, Haisheng[1,2];Gao, Jialong[1,2];Qin, Xiaoming[1,2];Zheng, Huina[1,2]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Key Lab Aquat Prod Proc & Safety, 1 Haida Rd, Zhanjiang, Guangdong, Peoples R China;[2]Guangdong Ocean Univ, Team Marine Food Nutr & Funct Res, Shenzhen Inst, Shenzhen, Peoples R China

年份：2025

卷号：60

期号：1

外文期刊名：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY

收录：SCI-EXPANDED(收录号：WOS:001442851400001)、、EI(收录号：20251318144419)、Scopus(收录号：2-s2.0-105001205605)、WOS

基金：This work was supported by the Guangdong Basic and Applied Basic Research Foundation (2024A1515010955), the Guangdong Province Modern Agricultural Industrial Technology System Innovation Team Construction Project (2024), the Modern Agricultural Industry Technology Research System of China (CARS-49), and the National Key R&D Program of China (2024YFD2401805).

语种：英文

外文关键词：abalone protein hydrolysates; limited enzymatic hydrolysis; functional properties; physicochemical properties; structural characterization

外文摘要：This study focused on preparing abalone protein hydrolysates from abalone muscle using papain and characterizing their functional, physicochemical, and structural properties. Abalone hydrolysates were stable in solubility across a hydrolysis degree range of 5.95%-14.46%. Hydrolysis notably enhanced foam capacity from 62% (Control) to 138% (APH-3). Emulsifying capacity and emulsion stability also improved significantly, increasing from 19.94 m(2)/g (Control) to 37.53 m(2)/g (APH-1) and from 19.59 min (Control) to 40.95 min (APH-1), respectively (p < .05). Moderate hydrolysis reduced protein molecular size, polydispersity index, and zeta potential, while increasing surface hydrophobicity, with APH-3 (DH 9.84%) showing the highest value. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed variations in protein composition with different hydrolysis degrees. Increased hydrolysis led to more disordered protein structures, affecting beta-sheet, beta-turn, and random coil proportions. Endogenous fluorescence and ultraviolet absorption intensities increased significantly (p < .05), whereas alpha-helix content and disulfide bonds decreased (p < .05). E-nose analysis indicated that hydrolysis degree significantly affected aromatic, hydride, alcohol, and methane aliphatic compounds. This study provides guidance for developing abalone protein hydrolysates with enhanced properties as potential functional foods. [GRAPHICS]