高压均质化：一种将不溶性豌豆蛋白分离物转化为可溶性聚集体的潜在技术。

High-pressure homogenization: A potential technique for transforming insoluble pea protein isolates into soluble aggregates.

机构信息

College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; Sericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, China.

Sericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, China.

出版信息

Food Chem. 2022 Dec 15;397:133684. doi: 10.1016/j.foodchem.2022.133684. Epub 2022 Jul 14.

DOI:10.1016/j.foodchem.2022.133684

PMID:35901613

Abstract

High-pressure homogenization (HPH) is a technique that impacts the aggregation of globular proteins. In this study, the effect of HPH (at a pressure of 30/50 MPa for three cycles) was investigated on the aggregation states and functional properties of insoluble commercial pea protein isolates (CPPI). Results showed that HPH significantly improved the solubility, foaming and emulsifying capacity of CPPI. Samples treated at 50 MPa demonstrated better foaming and emulsifying capacity than that at 30 MPa. Surface hydrophobicity, intrinsic fluorescence, SDS-PAGE and FTIR analysis revealed that insoluble precipitates/aggregates (most legumins included) of CPPI were broken down and converted into soluble aggregates. Low-pressure HPH (30 MPa) can break non-covalent bonds (hydrophobic interactions), whereas higher pressure (50 MPa) can further break covalent bonds (SS). The study sheds light on the mechanism of disruption of insoluble CPPI under HPH and proposes a method to enhance their techno-functional properties for application in food formulations.

摘要

高压均质（HPH）是一种影响球状蛋白质聚集的技术。在这项研究中，研究了 HPH（在 30/50 MPa 的压力下循环三次）对不溶性商业豌豆蛋白分离物（CPPI）的聚集状态和功能特性的影响。结果表明，HPH 显著提高了 CPPI 的溶解度、起泡性和乳化能力。在 50 MPa 下处理的样品比在 30 MPa 下处理的样品具有更好的起泡性和乳化能力。表面疏水性、内源荧光、SDS-PAGE 和 FTIR 分析表明，CPPI 的不溶性沉淀物/聚集物（包括大多数豆球蛋白）被分解并转化为可溶性聚集物。低压 HPH（30 MPa）可以破坏非共价键（疏水相互作用），而更高的压力（50 MPa）可以进一步破坏共价键（SS）。该研究揭示了 HPH 下不溶性 CPPI 破坏的机制，并提出了一种增强其技术功能特性的方法，以应用于食品配方。