Soluble-protein-aggregate-assisted improvements in heat-induced gel properties: Effect of genipin-mediated crosslinks on egg white protein

被引：17

作者：

Koyama, Shota ^{[1
,2
]}

Kodama, Daisuke ^{[3
]}

Tsujii, Yoshimasa ^{[1
,2
]}

Handa, Akihiro ^{[1
,4
]}

机构：

[1] Tokyo Univ Agr, Kewpie Res Div Egg Innovat, 1-1-1 Sakuragaoka, Tokyo, Tokyo 1568502, Japan

[2] Tokyo Univ Agr, Fac Appl Biosci, 1-1-1 Sakuragaoka, Tokyo, Tokyo 1568502, Japan

[3] Kewpie Corp, R&D Div, 2-5-7 Sengawa, Chofu, Tokyo 1820002, Japan

[4] Tokyo Denki Univ, Sch Sci & Engn, Ishizaka, Saitama 3500394, Japan

来源：

LWT-FOOD SCIENCE AND TECHNOLOGY | 2023年 / 184卷

关键词：

Protein complex; Gardenia blue; Gel strength; Dry-heat treatment; Crosslinker; GELLING PROPERTIES; FUNCTIONAL-PROPERTIES; MICROBIAL TRANSGLUTAMINASE; FOOD COLORANTS; DRY-HEAT; BLUE; OVALBUMIN;

D O I：

10.1016/j.lwt.2023.115079

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Genipin, a covalent crosslinker, has attracted significant attention from the food industry. Herein, the color, heat -induced gelling properties, and soluble aggregate character of the genipin-treated egg white were investigated to clarify the impact of soluble protein aggregates on the gel properties of egg white protein. After genipin pretreatment, the egg white protein turned dark blue and retained this color after heat-induced gelling. The genipin-pretreated egg white protein gel exhibited up to 2.9-fold and 13% higher breaking strength and strain, respectively, compared to non-treated egg white gel. The gel-breaking strength and strain correlated well with the color, before and after gelling. Gel electrophoresis, size exclusion, and anion exchange high-performance liquid chromatography revealed that a soluble protein aggregate with a negatively charged surface formed during pretreatment. The genipin-treated egg white protein formed a finely structured gel with high breaking strength and strain at all tested NaCl concentrations, indicating that the enhanced negative charge of the surface did not contribute to improving the gel properties. The soluble protein aggregates formed via covalent crosslinking are important for improving gel properties. The proposed method is a novel environmentally friendly method for enhancing the gel properties of egg white protein.

引用

页数：7

共 31 条

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