Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions
This study aimed to comparatively elucidate the composition structure and techno-functionality of flaxseed protein isolate (FPI), globulin (FG), and albumin (FA) fractions. The results showed that FA possessed smaller particle dimensions and superior protein solubility compared to that of FG (<i&...
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MDPI AG
2022-06-01
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author | Xiaopeng Qin Linbo Li Xiao Yu Qianchun Deng Qisen Xiang Yingying Zhu |
author_facet | Xiaopeng Qin Linbo Li Xiao Yu Qianchun Deng Qisen Xiang Yingying Zhu |
author_sort | Xiaopeng Qin |
collection | DOAJ |
description | This study aimed to comparatively elucidate the composition structure and techno-functionality of flaxseed protein isolate (FPI), globulin (FG), and albumin (FA) fractions. The results showed that FA possessed smaller particle dimensions and superior protein solubility compared to that of FG (<i>p</i> < 0.05) due to the lower molecular weight and hydrophobicity. FA and FG manifested lamellar structure and nearly spherical morphology, respectively, whereas FPI exhibited small lamellar strip structure packed by the blurring spheres. The Far-UV CD, FTIR spectrum, and intrinsic fluorescence confirmed more flexible conformation of FA than that of FG, followed by FPI. The preferential retention of free phenolic acids was observed for FA, leading to excellent antioxidant activities compared with that of FG in FPI (<i>p</i> < 0.05). FA contributed to the foaming properties of FPI, relying on the earlier interfacial adsorption and higher viscoelastic properties. FA displayed favorable emulsifying capacity but inferior stability due to the limited interfacial adsorption and deformation, as well as loose/porous interface. By comparison, an interlayer anchoring but no direct interface coating was observed for lipid droplets constructed by FG, thereby leading to preferable emulsion stability. However, FPI produced lipid droplets with dense interface owing to the effective migration of FA and FG from bulk phase, concomitant with the easy flocculation and coalescence. Thus, the techno-functionality of flaxseed protein could be tailed by modulating the retention of albumin fraction and specific phenolic acids. |
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spelling | doaj.art-69430640ab084ba2b739301f1833e2a02023-11-23T19:59:44ZengMDPI AGFoods2304-81582022-06-011113182010.3390/foods11131820Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein FractionsXiaopeng Qin0Linbo Li1Xiao Yu2Qianchun Deng3Qisen Xiang4Yingying Zhu5College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, ChinaCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, ChinaCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, ChinaOil Crops Research Institute, Chinese Academy of Agricultural Sciences, Wuhan 430062, ChinaCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, ChinaCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, ChinaThis study aimed to comparatively elucidate the composition structure and techno-functionality of flaxseed protein isolate (FPI), globulin (FG), and albumin (FA) fractions. The results showed that FA possessed smaller particle dimensions and superior protein solubility compared to that of FG (<i>p</i> < 0.05) due to the lower molecular weight and hydrophobicity. FA and FG manifested lamellar structure and nearly spherical morphology, respectively, whereas FPI exhibited small lamellar strip structure packed by the blurring spheres. The Far-UV CD, FTIR spectrum, and intrinsic fluorescence confirmed more flexible conformation of FA than that of FG, followed by FPI. The preferential retention of free phenolic acids was observed for FA, leading to excellent antioxidant activities compared with that of FG in FPI (<i>p</i> < 0.05). FA contributed to the foaming properties of FPI, relying on the earlier interfacial adsorption and higher viscoelastic properties. FA displayed favorable emulsifying capacity but inferior stability due to the limited interfacial adsorption and deformation, as well as loose/porous interface. By comparison, an interlayer anchoring but no direct interface coating was observed for lipid droplets constructed by FG, thereby leading to preferable emulsion stability. However, FPI produced lipid droplets with dense interface owing to the effective migration of FA and FG from bulk phase, concomitant with the easy flocculation and coalescence. Thus, the techno-functionality of flaxseed protein could be tailed by modulating the retention of albumin fraction and specific phenolic acids.https://www.mdpi.com/2304-8158/11/13/1820flaxseed protein fractionscomponent structuretechno-functionalityphenolic acidsinterfacial behavior |
spellingShingle | Xiaopeng Qin Linbo Li Xiao Yu Qianchun Deng Qisen Xiang Yingying Zhu Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions Foods flaxseed protein fractions component structure techno-functionality phenolic acids interfacial behavior |
title | Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions |
title_full | Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions |
title_fullStr | Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions |
title_full_unstemmed | Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions |
title_short | Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions |
title_sort | comparative composition structure and selected techno functional elucidation of flaxseed protein fractions |
topic | flaxseed protein fractions component structure techno-functionality phenolic acids interfacial behavior |
url | https://www.mdpi.com/2304-8158/11/13/1820 |
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