介质阻挡放电等离子体处理对大豆分离蛋白结构及凝胶特性的影响

    The effects of dielectric barrier discharge plasma treatment on the structure and gelling properties of soy protein isolate

    • 摘要: 低温等离子体技术作为利用高能活性粒子对蛋白结构修饰以改善其功能特性的手段,已广泛应用于蛋白等大分子物质的改性。以介质阻挡放电(DBD)等离子体处理大豆分离蛋白(SPI),对SPI的理化特性及结构进行分析,探究DBD等离子体处理对SPI结构及凝胶特性的影响。结果表明:与未处理样品相比,SPI经DBD等离子体处理40 s,凝胶性能达到最佳,其微观结构呈紧密的片状结构,硬度、黏附度分别增加2.63倍和5.98倍,随着处理时间的延长(60~120 s),其凝胶性能逐渐下降;对SPI结构的研究表明DBD等离子体处理对SPI一级和二级结构无显著影响,DBD等离子体介导产生的活性粒子氧化自由巯基为硫自由基,从而促进蛋白分子间二硫键的生成,形成稳固的三维网状结构,为SPI凝胶特性改善的主要原因,但过度氧化使SPI凝胶强度降低。因此,低温等离子体作为一种新型的非热加工技术在蛋白结构修饰以改善其功能特性方面具有巨大的应用前景,但控制低温等离子体处理参数以避免过度氧化带来的不利影响还需进一步研究。

       

      Abstract: As an effective technique to modify structure of protein with the active radical particles, cold plasma has been widely applied in modifying proteins to improve its functionality. The effects of dielectric barrier discharge (DBD) plasma treatment (20-120 s treatment time with 40 kV, 12 kHz) on the gelling properties of soy protein isolate (SPI) were investigated. Structural modification of SPI was determined using sodium dodecyl sulfate-polyacrylamide-gel electrophoresis (SDS-PAGE) and multi-spectroscopic analyses. The textural properties of the gels were determined by SEM, texture and dynamic rheological analyses. The results indicated that the SPI gel with 40 s plasma treatment displayed a compact sheet-like microstructure. Compared to untreated sample, it showed 2.63 and 5.98-fold increases in hardness and adhesiveness, which achieved excellent gel properties. A gradual weakening in gel properties was observed with prolonged treatment time (60-120 s). The results showed that the carbonyl content increased from the initial value of (2.39±0.09) μmol/g to (3.41±0.50) μmol/g with a mild oxidation induced by plasma treatment (40 s), and reached 4.36±0.16 μmol/g with an excessive oxidation induced by prolonged plasma treatment (120 s). The free sulfhydryl content gradually decreased from (4.49±0.13) μmol/g in untreated control samples to (3.86±0.09) μmol/g after exposure to plasma for 20 s, and further declined to (3.25±0.04) μmol/g after 40 s of plasma treatment. Further structure analyses in SPI showed that primary and secondary structures of glycinin were unaffected with plasma treatment. The underlying mechanism for enhancement of SPI gel ability was ascribed to the plasma-induced active radical particles, oxidated free sulfhydryl to sulfur radical, facilitating the generation of intermolecular disulfide bonds. However, excessive oxidation reduced the strength of SPI gel. Therefore, cold plasma, as a novel non-thermal processing technology, has great application prospects in protein structural modification to improve its functionality, but further research is required to control cold plasma processing parameters to avoid the adverse effects of excessive oxidation.

       

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