Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic Method
In this study, the internal relationships among oil bodies (OBs), the protein–phospholipid interactions in aqueous phase, oil–water interface behavior, and the stability of reconstituted OBs were analyzed from the bulk phase, interface, and macro perspectives, and the stability mechanism of OBs was...
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MDPI AG
2023-09-01
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Online Access: | https://www.mdpi.com/2304-8158/12/18/3446 |
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author | Chen Liu Fusheng Chen |
author_facet | Chen Liu Fusheng Chen |
author_sort | Chen Liu |
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description | In this study, the internal relationships among oil bodies (OBs), the protein–phospholipid interactions in aqueous phase, oil–water interface behavior, and the stability of reconstituted OBs were analyzed from the bulk phase, interface, and macro perspectives, and the stability mechanism of OBs was discussed. OB proteins and phospholipids were combined through hydrophobic and electrostatic interactions, resulting in the stretching of protein conformation. OB proteins and phospholipids act synergistically to increase interface pressure and the rate of increase in interface pressure with relatively stable elastic behavior, which is beneficial to the formation and stability of interfacial films. When OBs were reconstituted by an OB protein–phospholipid complex system, phospholipids bound to OB proteins through hydrophobic and electrostatic interactions. OB proteins and phospholipids uniformly covered the oil droplet surface of reconstituted OBs to form a stable interfacial film, which maintained the stability of OBs. The addition of phospholipids significantly reduced the particle size of OBs prepared by OB proteins in a dose-dependent manner, and particle size decreased with the increase in phospholipid content (<i>p</i> < 0.05). Phospholipids increased the net surface charge, enhanced electrostatic repulsion, and improved the physicochemical stability of reconstituted OBs. The stability mechanism elucidated in this study provides a theoretical basis for the demulsification of peanut OBs. |
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spelling | doaj.art-453c118a4d2f4b108841ca4bf300457b2023-11-19T10:43:14ZengMDPI AGFoods2304-81582023-09-011218344610.3390/foods12183446Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic MethodChen Liu0Fusheng Chen1College of Biology and Food, Shangqiu Normal University, Shangqiu 476000, ChinaCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, ChinaIn this study, the internal relationships among oil bodies (OBs), the protein–phospholipid interactions in aqueous phase, oil–water interface behavior, and the stability of reconstituted OBs were analyzed from the bulk phase, interface, and macro perspectives, and the stability mechanism of OBs was discussed. OB proteins and phospholipids were combined through hydrophobic and electrostatic interactions, resulting in the stretching of protein conformation. OB proteins and phospholipids act synergistically to increase interface pressure and the rate of increase in interface pressure with relatively stable elastic behavior, which is beneficial to the formation and stability of interfacial films. When OBs were reconstituted by an OB protein–phospholipid complex system, phospholipids bound to OB proteins through hydrophobic and electrostatic interactions. OB proteins and phospholipids uniformly covered the oil droplet surface of reconstituted OBs to form a stable interfacial film, which maintained the stability of OBs. The addition of phospholipids significantly reduced the particle size of OBs prepared by OB proteins in a dose-dependent manner, and particle size decreased with the increase in phospholipid content (<i>p</i> < 0.05). Phospholipids increased the net surface charge, enhanced electrostatic repulsion, and improved the physicochemical stability of reconstituted OBs. The stability mechanism elucidated in this study provides a theoretical basis for the demulsification of peanut OBs.https://www.mdpi.com/2304-8158/12/18/3446stability mechanismpeanut OBsproteinphospholipidinteraction |
spellingShingle | Chen Liu Fusheng Chen Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic Method Foods stability mechanism peanut OBs protein phospholipid interaction |
title | Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic Method |
title_full | Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic Method |
title_fullStr | Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic Method |
title_full_unstemmed | Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic Method |
title_short | Study on the Stability Mechanism of Peanut OBs Extracted with the Aqueous Enzymatic Method |
title_sort | study on the stability mechanism of peanut obs extracted with the aqueous enzymatic method |
topic | stability mechanism peanut OBs protein phospholipid interaction |
url | https://www.mdpi.com/2304-8158/12/18/3446 |
work_keys_str_mv | AT chenliu studyonthestabilitymechanismofpeanutobsextractedwiththeaqueousenzymaticmethod AT fushengchen studyonthestabilitymechanismofpeanutobsextractedwiththeaqueousenzymaticmethod |