Stephan Buecker , Elena Leeb , Monika Gibis , Jochen Weiss
{"title":"研究节肢动物板蓝根提取物与高甲氧基化果胶、低甲氧基化果胶和λ-卡拉胶的相互作用力和络合物的形成","authors":"Stephan Buecker , Elena Leeb , Monika Gibis , Jochen Weiss","doi":"10.1016/j.foodhyd.2024.110774","DOIUrl":null,"url":null,"abstract":"<div><div>Numerous complexation mechanisms have been explored to stabilize the blue pigment phycocyanin from <em>Arthrospira platensis</em>. However, previous studies have primarily focused on the application of various methods rather than delving into molecular interactions. This study compared the interactions of citrus pectins with a high degree of esterification and a low degree of esterification as well as lambda-carrageenan. The goal was to identify a molecule suitable for complexation that maintains stability against heating in terms of color and colloidal stability. Size measurements employing dynamic light scattering and static light scattering, as well as characterization of properties such as zeta potential, were performed for the various complexes. Moreover, the complexation mechanism was investigated by isothermal titration calorimetry and computational blind docking. Weak complexes were formed at neutral pH, driven by an entropy gain facilitated by hydrophobic interactions and van der Waals forces between non-polar groups. It seems that this step is essential in achieving structures with a core shell formation. A decrease in pH resulted in intensified complex formation driven by enhanced electrostatic interactions, leading to a shift in enthalpy from values between −4 and −23 kJ٠mol<sup>−1</sup> to values between −15 and −25 kJ٠mol<sup>−1</sup>. Multiple binding sites were identified across the protein surfaces, primarily involving polar groups. Interactions with arginine were particularly significant, exhibiting 28 interaction counts compared to only 8 for threonine, despite threonine's greater prominence in the protein sequence. These interactions are thought to compete with interactions between allophycocyanin and c-phycocyanin subunits and protein chromophore interactions, resulting in a color shift. The study highlights the importance of selecting the appropriate biopolymer for optimal performance, considering the delicate balance between strong interactions and bulkiness to prevent complex precipitation.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110774"},"PeriodicalIF":11.0000,"publicationDate":"2024-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Study of interactive forces and complex formation from Arthrospira platensis extract with high methoxylated pectin, low methoxylated pectin and lambda-carrageenan\",\"authors\":\"Stephan Buecker , Elena Leeb , Monika Gibis , Jochen Weiss\",\"doi\":\"10.1016/j.foodhyd.2024.110774\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Numerous complexation mechanisms have been explored to stabilize the blue pigment phycocyanin from <em>Arthrospira platensis</em>. However, previous studies have primarily focused on the application of various methods rather than delving into molecular interactions. This study compared the interactions of citrus pectins with a high degree of esterification and a low degree of esterification as well as lambda-carrageenan. The goal was to identify a molecule suitable for complexation that maintains stability against heating in terms of color and colloidal stability. Size measurements employing dynamic light scattering and static light scattering, as well as characterization of properties such as zeta potential, were performed for the various complexes. Moreover, the complexation mechanism was investigated by isothermal titration calorimetry and computational blind docking. Weak complexes were formed at neutral pH, driven by an entropy gain facilitated by hydrophobic interactions and van der Waals forces between non-polar groups. It seems that this step is essential in achieving structures with a core shell formation. A decrease in pH resulted in intensified complex formation driven by enhanced electrostatic interactions, leading to a shift in enthalpy from values between −4 and −23 kJ٠mol<sup>−1</sup> to values between −15 and −25 kJ٠mol<sup>−1</sup>. Multiple binding sites were identified across the protein surfaces, primarily involving polar groups. Interactions with arginine were particularly significant, exhibiting 28 interaction counts compared to only 8 for threonine, despite threonine's greater prominence in the protein sequence. These interactions are thought to compete with interactions between allophycocyanin and c-phycocyanin subunits and protein chromophore interactions, resulting in a color shift. The study highlights the importance of selecting the appropriate biopolymer for optimal performance, considering the delicate balance between strong interactions and bulkiness to prevent complex precipitation.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"160 \",\"pages\":\"Article 110774\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2024-10-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Hydrocolloids\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0268005X24010488\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X24010488","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Study of interactive forces and complex formation from Arthrospira platensis extract with high methoxylated pectin, low methoxylated pectin and lambda-carrageenan
Numerous complexation mechanisms have been explored to stabilize the blue pigment phycocyanin from Arthrospira platensis. However, previous studies have primarily focused on the application of various methods rather than delving into molecular interactions. This study compared the interactions of citrus pectins with a high degree of esterification and a low degree of esterification as well as lambda-carrageenan. The goal was to identify a molecule suitable for complexation that maintains stability against heating in terms of color and colloidal stability. Size measurements employing dynamic light scattering and static light scattering, as well as characterization of properties such as zeta potential, were performed for the various complexes. Moreover, the complexation mechanism was investigated by isothermal titration calorimetry and computational blind docking. Weak complexes were formed at neutral pH, driven by an entropy gain facilitated by hydrophobic interactions and van der Waals forces between non-polar groups. It seems that this step is essential in achieving structures with a core shell formation. A decrease in pH resulted in intensified complex formation driven by enhanced electrostatic interactions, leading to a shift in enthalpy from values between −4 and −23 kJ٠mol−1 to values between −15 and −25 kJ٠mol−1. Multiple binding sites were identified across the protein surfaces, primarily involving polar groups. Interactions with arginine were particularly significant, exhibiting 28 interaction counts compared to only 8 for threonine, despite threonine's greater prominence in the protein sequence. These interactions are thought to compete with interactions between allophycocyanin and c-phycocyanin subunits and protein chromophore interactions, resulting in a color shift. The study highlights the importance of selecting the appropriate biopolymer for optimal performance, considering the delicate balance between strong interactions and bulkiness to prevent complex precipitation.
期刊介绍:
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.