Emulsifying and Foaming Properties of Different Protein Fractions Obtained from a Novel Lupin Variety AluProt‐CGNA^® (Lupinus luteus)

Abstract

The use of vegetable proteins as food ingredient is becoming increasingly important due to their high versatility and environmental acceptability. This work describes a chemical characterization and techno-functional properties (emulsifying and foaming properties) of 3 protein fractions obtained from a protein-rich novel lupin variety, AluProt-CGNA(®) . This nongenetically modified variety have a great protein content in dehulled seeds (60.6 g protein/100 g, dry matter), which is higher than soybean and other lupin varieties. A simple procedure was utilized to obtain 3 different fractions by using alkali solubilization and isoelectric precipitation. Fractions 1 and 3 were mainly composed of protein and polysaccharides (NNE), whereas fraction 2 was mainly composed by protein (97%, w/w). Fraction 3 presented interesting and potential foaming properties in comparison to the other fractions evaluated in the study. Besides, its solubility, foaming and emulsifying capacity were practically not affected by pH variations. The 3 fractions also presented good emulsion stability, reaching values above a 95%. SDS-PAGE showed that fractions 1 and 2 contained mainly conglutin α, β, and δ, but in different ratios, whereas fraction 3 contained mainly conglutin γ and albumins. The results of this work will provide better understanding for the utilization of each protein fractions as potential ingredients in food industry.

Antimicrobial and Functional Properties of Duckweed (Wolffia globosa) Protein and Peptide Extracts Prepared by Ultrasound-Assisted Extraction

“…Greater interactions with the lipid phase were attributed to the higher ES values of the PE and PS [ 34 ]. The EC and ES of the PE and PS were comparable to the protein isolate from the lupin with the highest EC (63%) and ES (99%) at pH 3 reported by Burgos-Diaz et al [ 11 ]. The PE and PS both showed good functionality with high solubility and emulsifying properties, as well as potential for further use as ingredients in functional foods.…”

“…According to the results regarding the PE solubilities, the lowest solubility of proteins relates to a pI value where the net charge of the molecules is zero and repulsive forces between protein molecules are reduced, promoting their aggregation and precipitation. At pH values lower and higher than this pI, proteins carry positive and negative net charges, respectively, and exhibit higher solubility [ 11 ]. This solubility behavior was also reported for proteins derived from other legumes such as chickpeas [ 24 ], lentils [ 25 ] and lupins [ 26 ].…”

“…Carbohydrates in the PS inhibited precipitation of proteins at the isoelectric point (pI). Burgos-Diaz et al [ 11 ] reported that the positive charge of proteins interacted with the negative charge of polysaccharides to form a stable electrostatic complex when the pH decreased below the pI of proteins, resulting in improvement of protein solubility. The oligosaccharide chain of polysaccharides also contributed to the solubility of proteins [ 27 ].…”

“…In addition, proteins are used as essential ingredients in food applications due to their biological activities and functional properties such as the formation of emulsions and foams [ 10 ]. The protein isolate obtained from the protein-rich lupin variety AluProt-CGNA ® (LPIA) at pH 3 showed high emulsion capacity (%EC) and emulsion stability (%ES) values of 63% and 99%, respectively [ 11 ]. LPIA also exhibited potential use as a stabilizer for oil-in-water (O/W) Pickering emulsions, with more beneficial applications in food industries [ 12 ].…”

Extraction, purification by cation exchange supermacroporous cryogel and physico‐chemical characterization of γ‐conglutin from lupin seeds (Lupinus albus L.)

“…It has been reported that lupin proteins present technological properties (foaming, emulsifying, and gelling properties) for applications in the food and pharmaceutical industries [5,6]. The total protein content corresponds to ca.…”