期刊
JOURNAL OF FOOD SCIENCE
卷 84, 期 8, 页码 2242-2249出版社
WILEY
DOI: 10.1111/1750-3841.14734
关键词
aggregate; foaming properties; microfluidization; pea albumins; thermal denaturation
资金
- Conseil Regional de Bourgogne through the plan d'actions regionales pour l'innovation (PARI)
- European Union through the PO FEDER-FSE Bourgogne
The effect of dynamic high-pressure treatment, also named microfluidization, on the surface properties of thermal pea albumin aggregates (AA) and their foaming ability was investigated at pH 3, 5, and 7. The solubility of albumin particles was not affected by the increase in microfluidization pressure from 70 to 130 MPa. Particle charge depended only on the pH, whereas protein surface hydrophobicity was stable at pH 5, decreased at pH 3, but increased at pH 7 after microfluidization treatment and with the applied pressure. Surface tension of AA measured at air/water interface was favorably affected by the microfluidization treatment at each pH preferentially due to size reduction and increased flexibility of protein particles. The foaming capacity and stability of AA depended on the pH conditions and the microfluidization treatment. The high-pressure treatment had little influence in foaming properties at acidic pHs, probably related to a more compact form of AA at these pHs. At neutral pH, the foaming properties of pea AA were strongly influenced by their surface properties and size associated with significant modifications in AA structure with microfluidization. Changes in albumin aggregate characteristics with pH and microfluidization pressure are also expected to modulate other techno-functional properties, such as emulsifying property. Practical Application Albumins are known for their interesting nutritional values because they are rich in essential amino acids. This fraction is not currently marketed as a protein isolate for human consumption, but can be considered as a potential new vegetable protein ingredient. This document demonstrated that heat treatment or dynamic high-pressure technology can control the foaming properties of this protein for possible use in expanded foods.
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