Functionalising insoluble pea protein aggregates using high-pressure homogenisation: Effects on physicochemical, microstructural and functional properties

IF 5.6 3区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY

Food Structure-Netherlands Pub Date : 2022-10-01 DOI:10.1016/j.foostr.2022.100298

Kian Siang Ong , Jie Hong Chiang , Shaun Yong Jie Sim , David Liebl , Mufeeda Madathummal , Christiani Jeyakumar Henry

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引用次数: 2

Abstract

Commercial plant protein isolates contain a large fraction of non-functional proteins due to the harsh processing conditions used. Therefore, greater value can be unlocked by functionalising these “inert” plant proteins. Using commercial insoluble pea protein isolate (I-PPI) as an example, this study demonstrates the application of high-pressure homogenisation (HPH) as a physical method to improve the techno-functionality of I-PPI. The dispersions were HPH-treated at 60, 120, or 180 MPa for one, three, and five pressure cycles. HPH treatments resulted in decreased particle size (from 16.7 ± 1.3–9.4 ± 0.2 µm at 60 MPa) and increased zeta-potential. Microstructural observations revealed the formation of smaller aggregate clusters and flake-like structures after HPH treatments. The protein solubility of I-PPI (15.9 ± 2.0 %) under acidic conditions (pH 2) significantly increased at all HPH treatment levels, with the greatest increase at 120 MPa for 5 passes (27.2 ± 2.0 %). Remarkably, the non-gelling I-PPI was able to form self-standing gels (15 % w/w) after HPH treatments, with the greatest gel strength observed at 180 MPa. The emulsifying and foaming stability of HPH-treated I-PPI increased from 60 to 120 MPa but decreased at 180 MPa. Overall, our results demonstrate a key paradigm in protein modification: transforming insoluble plant proteins into functional protein ingredients.

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使用高压均质化技术功能化不溶性豌豆蛋白聚集体:对物理化学、微观结构和功能特性的影响

由于使用了苛刻的加工条件，商业植物蛋白分离物含有很大一部分非功能蛋白。因此，通过使这些“惰性”植物蛋白功能化，可以释放出更大的价值。以商品不溶性豌豆分离蛋白(I-PPI)为例，本研究展示了高压均质(HPH)作为一种物理方法的应用，以提高I-PPI的技术功能。分散体分别在60、120或180 MPa高压下进行1、3和5个压力循环处理。高ph处理导致颗粒尺寸减小(在60 MPa下从16.7±1.3µm到9.4±0.2µm)， ζ电位增加。显微结构观察显示，HPH处理后形成较小的聚集团簇和片状结构。在酸性条件(pH 2)下，所有HPH处理水平下I-PPI的蛋白溶解度均显著增加(15.9±2.0%)，其中在120 MPa处理5次时最大(27.2±2.0%)。值得注意的是，非胶凝I-PPI在HPH处理后能够形成自立凝胶(15% w/w)，在180 MPa时凝胶强度最大。hph处理后的I-PPI的乳化和发泡稳定性在60 ~ 120 MPa范围内有所提高，但在180 MPa范围内有所下降。总的来说，我们的研究结果证明了蛋白质修饰的一个关键范例:将不溶性植物蛋白转化为功能性蛋白质成分。

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来源期刊

Food Structure-Netherlands Chemical Engineering-Bioengineering

CiteScore

7.20

自引率

0.00%

发文量

期刊介绍： Food Structure is the premier international forum devoted to the publication of high-quality original research on food structure. The focus of this journal is on food structure in the context of its relationship with molecular composition, processing and macroscopic properties (e.g., shelf stability, sensory properties, etc.). Manuscripts that only report qualitative findings and micrographs and that lack sound hypothesis-driven, quantitative structure-function research are not accepted. Significance of the research findings for the food science community and/or industry must also be highlighted.