Factors determining the physical properties of protein foams

Foegeding, E. Allen; Luck, P.J.; Davis, J.

doi:10.1016/j.foodhyd.2005.03.014

Cited by 316 publications

(215 citation statements)

References 50 publications

Supporting

Mentioning

198

Contrasting

Unclassified

Order By: Relevance

“…Similar to phenomena influencing emulsifying properties of MLPF hydrolysates, conformational changes induced by enzymatic cleavage led to the generation of small peptides and exposure of surface-stabilising residues resulting in improved foamability due to rapid diffusion and stabilisation of the interfacial layer [50]. In analogy to the results of the single enzyme hydrolyses, the combination of enzymes resulted in deteriorated foamability of MLPF hydrolysates at neutral and alkaline pH, which might be ascribed to the higher repulsive forces and lower elasticity of the interfacial layer at pH 7-9 in comparison to the isoelectric point around pH 4 [61].…”

Section: Emulsifying and Foaming Propertiesmentioning

confidence: 98%

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

View full text Add to dashboard Cite

Enzymatic hydrolysis of migratory locust (Locusta migratoria L.) protein flour (MLPF) was investigated as a method to improve the techno-functional properties. Experiments were conducted under variation of the applied proteases (Alcalase, Neutrase, Flavourzyme, Papain) or combinations thereof, enzyme-substrate ratio (0.05-1.0% w/w), heat pre-treatment (60-80 °C; 15-60 min), and hydrolysis time (0-24 h). Protein degradation was monitored in terms of degree of hydrolysis (DH) and SDS-PAGE. Solubility, emulsifying, foaming and water/oil binding properties of the hydrolysates were determined. In comparison to the control (DH = 5%), hydrolysis resulted in considerably higher DH values up to 42%. SDS-PAGE profiles revealed a steady decrease of bands between 25 and 75 kDa and an increase of low molecular weight bands (10-15 kDa). However, different heat pre-treatments resulted in impaired hydrolytic cleavage as evidenced by lower DH values. Protein solubility of MLPF hydrolysates was improved over a broad pH range from initially 10-22% up to 55% at alkaline conditions. Furthermore, hydrolysis resulted in enhanced emulsifying activity (54%) at pH 7, improved foamability (326%) at pH 3 and advanced oil binding capacity. The results of this study have clearly demonstrated the potential of targeted enzymatic degradation to improve the techno-functionality of migratory locust protein in order to produce tailored insect-based ingredients for the use in food applications.

show abstract

Section: Emulsifying and Foaming Propertiesmentioning

confidence: 98%

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

View full text Add to dashboard Cite

show abstract

“…Foam production involves the generation of a protein film surrounding a gas bubble, and the packing of gas bubbles into an overall structure. The spontaneous behavior of proteins in aqueous solutions to adsorb to the air-water interface, causing the lowering of the interfacial (surface) tension, is of central importance for foaming properties (Foegeding et al 2006). Protein hydrolysis usually presents a positive effect on foaming capacity (Were et al 1997;Tsumura et al 2005;Sinha et al 2007;Jamdar et al 2010), since the generated peptides usually present an increased adsorption rate due to their faster diffusion to the interface when compared to the non-hydrolyzed proteins (Foegeding et al 2006;Martínez et al 2009).…”

Section: Foaming and Emulsifying Propertiesmentioning

confidence: 99%

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

View full text Add to dashboard Cite

Soybean proteins are widely used as nutritional and functional food ingredients. This investigation evaluated through a 2 3 central composite design the effect of three variables (pH, temperature and enzyme/substrate (E/S) ratio) on the production of soy protein isolate (SPI) hydrolysates with a microbial protease. Soluble peptides, antioxidant activity, and foaming and emulsifying capabilities of the hydrolysates were analyzed. All variables, as well as their interactions, were significant for the soluble peptides content of SPI hydrolysates. Optimal conditions for obtaining soluble peptides were around 30-35°C, pH 6.5-9.5, and E/S ratios of 1,650-6,300 U g −1 . SPI hydrolysates produced at 30-45°C, pH 8.0-9.5, and E/S ratios of 4,000-8,000 U g −1 showed higher capacity to scavenge the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical. Models for soluble peptides and ABTS activity of hydrolysates were obtained. In the range studied, the variables had not significant influence on the ability of hydrolysates to scavenge the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical. SPI hydrolysates also presented reducing power and ability to chelate iron. Hydrolysis temperature was significant for the Fe 2+ -chelating ability of hydrolysates. Temperature of hydrolysis was significant for the foaming capacity of hydrolysates, with higher values observed at 45°C and 8,000 U g −1 . For emulsifying capacity, only E/S ratio presented a significant effect. Temperature and E/S ratio appeared to be more significant variables influencing the properties of the SPI hydrolysates. The results of this study indicate that specific hydrolysis conditions should be selected to obtain SPI hydrolysates with preferred characteristics.

show abstract

“…inherent nature of the protein) as well as extrinsic factors (e.g. pH, ionic environment and heat) influence the formation and stability of a foam [10,13,14,[20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Skim milk powders with enhanced foaming and steam-frothing properties

Augustin¹,

Clarke²

2008

Dairy Sci. Technol.

View full text Add to dashboard Cite

-The effects of citrate addition to milks on the stability of milk foams formed by two aeration processes, whipping at room temperature and by steam-frothing, were examined. Citrate addition (0.1-0.5 mol added citrate·kg −1 milk solids non-fat) improved the whipping properties of milks reconstituted from conventional low-heat (72 • C for 30 s) and high-heat (85 • C for 30 min) powders. This effect was attributed to the role of citrate in dissociating casein micelles. However, while citrate addition (0.1-0.2 mol added citrate·kg −1 milk solids non-fat) improved the steamfrothing properties of milks reconstituted from conventional low-heat milk powder it did not improve those of milks made from corresponding high-heat milk powders. Similar effects of citrate addition on foaming and stream-frothing properties were obtained when the salts were added to skim milk concentrate prior to drying. The citrated milk powders are alternatives to physical blends of conventional skim milk powders and citrate salts for enhancing the foaming properties of milks at both low and high application temperatures. milk powder / foaming / stream-frothing / casein micelle / citrate

show abstract

Factors determining the physical properties of protein foams

Cited by 316 publications

References 50 publications

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Skim milk powders with enhanced foaming and steam-frothing properties

Contact Info

Product

Resources

About