4.7 Article

A comprehensive research on Lactone Sophorolipid (LSL) and Soy Protein Isolate (SPI) interacting mixture

期刊

JOURNAL OF MOLECULAR LIQUIDS
卷 339, 期 -, 页码 -

出版社

ELSEVIER
DOI: 10.1016/j.molliq.2021.117239

关键词

Lactone Sophorolipid (LSL); Soy Protein Isolate (SPI); Surface properties; Foam; Interaction mechanism

资金

  1. National Natural Science Foundation of China [22073039]
  2. Teaching Reform Project of Shandong Province [M2020059, SDYAL19059, 201902195011]

向作者/读者索取更多资源

This study comprehensively investigated the interaction mode and properties of LSL and SPI composite systems, revealing different performance optimizations under various mass ratios. The combination of LSL and SPI altered the protein structure, enhancing our understanding of the interaction mechanism between the two components.
Soy protein isolate (SPI) is a promising biological material, and lactone sophorolipid (LSL) is a non-toxic, completely biodegradable amphiphilic functional biosurfactant. A comprehensive research of interaction mode and mechanism on LSL and SPI composite system was studied using surface tension, turbidity, fluorescence spectroscopy, ultraviolet-visible (UV-Vis) spectroscopy, circular dichroism (CD) spectroscopy, dynamic light scattering (DLS), isothermal microcalorimetric titration (ITC) and molecular docking methods. The properties of surface activity, foam stability, antibacterial ability and so on were evaluated in detail. Compared with a single pure substance, the performance of the composite system shows different performance optimizations in different aspects. For the SPI/LSL systems with different mass ratios studied, the surface activity, foaming performance and foam stability of the composite system with a mass ratio of 1:50 are more prominent than those of other ratios. The fluorescence distribution showed the increase of LSL leading to a significant change in the fluorescence distribution of SPI, the quenching mechanism is mainly static quenching mechanism, and the combination of LSL and SPI is an spontaneous endothermic process. UV-Vis spectroscopy showed that LSL changed the conformation of SPI. The CD spectrum indicated that the combination of LSL and SPI increases the alpha-helical structure of protein, and is beneficial to the secondary structure of protein. The molecular model presents the conformation of the SPI/LSL complex, indicating that the hydrophobic force and hydrogen bonds are considered to be the main interaction forces between SPI and LSL, which may lead to the flexible conformation of the protein. This research enriches our understanding of the interaction mechanism between SPI and LSL, and provides some important and interesting information for the development and application of biosurfactant-protein mixed systems with environmentally friendly, non-toxic and non-polluting properties. (C) 2021 Elsevier B.V. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据