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1.
Food Chem ; 372: 131275, 2022 Mar 15.
Article in English | MEDLINE | ID: mdl-34638058

ABSTRACT

Sunflower protein isolate obtained from industrially de-oiled press cake was treated with non-thermal microwave, aiming to investigate how structure and emulsifying properties were affected. Our results indicated that the content of polar amino acids was decreased and solubility and surface hydrophobicity were altered upon exposure to non-thermal microwave. Higher solubility and surface hydrophobicity of the samples treated with defrost mode and also 350 W were accompanied by a smaller size and lower uniformity of the oil droplets compared to the control and other samples. Non-thermal microwave treatment improved the emulsion stability by 1.43 times and defrost mode treated sample had the lowest stability index after 120 min. Interfacial dilatational rheology measurements revealed that 70 and 350 W treated samples created higher elastic, less stretchable solid-like layer at the O/W interface in comparison with defrost mode treated and control samples. Consequently, non-thermal microwave treatment could be considered as a promising simple, fast, and "green" protein modification technique.


Subject(s)
Helianthus , Emulsifying Agents , Emulsions , Hydrophobic and Hydrophilic Interactions , Oils , Rheology , Solubility , Water
2.
J Sci Food Agric ; 99(15): 6922-6930, 2019 Dec.
Article in English | MEDLINE | ID: mdl-31393601

ABSTRACT

BACKGROUND: The potential use of polyphenols to improve the functional characteristics of dairy products has gained much attention. However, the effects of the polyphenols on naturally occurring enzymes in milk have not been studied extensively. Excess plasmin activity in dairy products might result in several quality defects. The objective of this study was to assess the ability of polyphenols to inhibit plasmin in milk using a molecular and kinetic approach. RESULTS: Epicatechin gallate (ECG), epigallocatechin gallate (EGCG), quercetin (QUER), and myricetin (MYR) caused a significant decrease in plasmin activity by 60, 86, 65, and 90%, respectively. The inhibition rates were alleviated in the presence of milk proteins. EGCG, QUER, and MYR, exhibited noncompetitive inhibition against plasmin, whereas ECG caused a mixed-type inhibition. A decrease in the random structure of plasmin upon the complex formation with ECG, EGCG, QUER, and MYR was found. The other phenolics that were evaluated did not cause any significant changes in plasmin conformation. The observed inhibitory phenolic-plasmin interactions were dominated by H-bonds and electrostatic attractions. Green tea extract (GTE) rich in catechins also inhibited plasmin activity in the milk. CONCLUSION: Significant changes in the secondary structure of plasmin upon binding of ECG, EGCG, QUER, and MYR led to diminished plasmin activity both in the absence and presence of milk proteins. These flavonoids with promising plasmin inhibitory potential could be used in new dairy formulations leading to controlled undesired consequences of plasmin activity. © 2019 Society of Chemical Industry.


Subject(s)
Antifibrinolytic Agents/chemistry , Camellia sinensis/chemistry , Milk/enzymology , Plant Extracts/chemistry , Polyphenols/chemistry , Animals , Catechin/analogs & derivatives , Catechin/chemistry , Cattle , Fibrinolysin/chemistry , Kinetics , Milk/chemistry
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