Exploring the influence of different enzymes on soy hull polysaccharide emulsion stabilization: A study on interfacial behavior and structural changes.
Autor: | Xu Y; College of Food Science and Technology, Bohai University, Jinzhou, 121013, China., Wang S; College of Food Science and Technology, Bohai University, Jinzhou, 121013, China.; Grain and Cereal Food Bio-efficient Transformation Engineering Research Center of Liaoning Province, Jinzhou, 121013, China.. Electronic address: wsnname@163.com., Xin L; College of Food Science and Technology, Bohai University, Jinzhou, 121013, China., Zhang L; College of Food Science and Technology, Bohai University, Jinzhou, 121013, China., Yang L; College of Food Science and Technology, Bohai University, Jinzhou, 121013, China.; Grain and Cereal Food Bio-efficient Transformation Engineering Research Center of Liaoning Province, Jinzhou, 121013, China., Wang P; College of Food Science and Technology, Bohai University, Jinzhou, 121013, China.; Grain and Cereal Food Bio-efficient Transformation Engineering Research Center of Liaoning Province, Jinzhou, 121013, China., Liu H; College of Food Science and Technology, Bohai University, Jinzhou, 121013, China.; Grain and Cereal Food Bio-efficient Transformation Engineering Research Center of Liaoning Province, Jinzhou, 121013, China. |
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Jazyk: | angličtina |
Zdroj: | Food chemistry [Food Chem] 2025 Jan 15; Vol. 463 (Pt 1), pp. 141147. Date of Electronic Publication: 2024 Sep 04. |
DOI: | 10.1016/j.foodchem.2024.141147 |
Abstrakt: | The interfacial behavior of soy hull polysaccharide (SHP) at the oil-water interface and the stabilization mechanism of high internal phase emulsion (HIPE) with three enzymes (α-amylase, trypsin and papain) were investigated. The diameter of the α-amylase-treated emulsion was the minimum at 40 min, indicating that the carbohydrate portions of SHP form a thick layer on the surface of the droplet to prevent aggregation. Moreover, Raman spectroscopy revealed significantly higher levels of disordered content of SHP emulsion treated with α-amylase at 60 min, potentially affecting the directional movement of SHP molecules in the emulsion. Conversely, the content of β-sheet and β-turn was lower than trypsin and papain, possibly due to ion-dipole interaction between the polar group residues within SHP and ions, or protonation with H + . Competing Interests: Declaration of competing interest The authors declare no competing financial interests. (Copyright © 2024. Published by Elsevier Ltd.) |
Databáze: | MEDLINE |
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