White lupin protein isolate as a foaming agent

1998 ◽  
Vol 207 (2) ◽  
pp. 91-96 ◽  
Author(s):  
A. Raymundo ◽  
J. Empis ◽  
I. Sousa
Foods ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 230 ◽  
Author(s):  
Martin Vogelsang-O’Dwyer ◽  
Juergen Bez ◽  
Iben Lykke Petersen ◽  
Marcel Skejovic Joehnke ◽  
Andreas Detzel ◽  
...  

Similarly prepared protein isolates from blue lupin (Lupinus angustifolius) and white lupin (L. albus) were assessed in relation to their composition, functional properties, nutritional attributes and environmental impacts. Blue lupin protein isolate (BLPI) and white lupin protein isolate (WLPI) were found to be quite similar in composition, although differences in the electrophoretic protein profiles were apparent. Both lupin protein isolates (LPIs) had good protein solubility (76.9% for BLPI and 69.8% for WLPI at pH 7) and foaming properties. However, a remarkable difference in heat gelation performance was observed between BLPI and WLPI. WLPI had a minimum gelling concentration of 7% protein, whereas BLPI required 23% protein in order to form a gel. WLPI also resulted in stronger gels over a range of concentrations compared to BLPI. Nutritional properties of both LPIs were similar, with no significant differences in in vitro protein digestibility (IVPD), and both had very low trypsin inhibitor activity (TIA) and fermentable oligo-, di- and monosaccharides, and polyols (FODMAP) content. The amino acid profiles of both LPIs were also similar, with sulfur-containing amino acids (SAAs) being the limiting amino acid in each case. Environmental impacts revealed by the life cycle assessment (LCA) were almost identical for BLPI and WLPI, and in most categories the LPIs demonstrated considerably better performance per kg protein when compared to cow’s whole milk powder.


1994 ◽  
Vol 72 (6) ◽  
pp. 865-871 ◽  
Author(s):  
D.S. Petterson ◽  
B. SandstrÖm ◽  
Å. Cederblad

The absorption of Zn from a lupin (Lupinus angustifolius) milk fortified with Ca, a bread containing lupin flour (230 g/kg), a sauce containing lupin flour and a sauce containing a lupin-protein isolate was determined in humans by measuring the whole-body retention of radioisotope from meals labelled with 0·02 MBq 65Zn, allowing for endogenous excretion of Zn, after 14 d. The absorption of Zn from the Ca-enriched milk (16·2%) and the bread made with lupin flour (27·0%) was similar to literature figures for comparable soya-bean products. The absorption from composite meals made with lupin flour (28·2%) and protein isolate (32·7%) was significantly higher than that reported for comparable soya-bean products. In a second experiment the absorption of Zn from a lupin-milk base and a soya-bean-milk base was compared with that from Ca-supplemented bases. The absorption of Zn from the lupin-milk base (26·3%) was significantly higher than from the soya-bean-milk base (17·6%), and neither was significantly altered by the addition of Ca. Overall the absorption of Zn from lupin-protein foods was found to be higher than from comparable soya-bean products. Lupin milk could be an attractive alternative to soya-bean milk for infant formulas.


2007 ◽  
Vol 101 (1) ◽  
pp. 57-64 ◽  
Author(s):  
Georgios Doxastakis ◽  
Maria Papageorgiou ◽  
Dimitra Mandalou ◽  
Maria Irakli ◽  
Evdoxia Papalamprou ◽  
...  

Foods ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 312
Author(s):  
Eduardo Morales ◽  
César Burgos-Díaz ◽  
Rommy N. Zúñiga ◽  
Johanna Jorkowski ◽  
Marcela Quilaqueo ◽  
...  

The utilization of astaxanthin in food processing is considered to be narrow because of its substandard solubility in aqueous matrices and the instability of chemical compounds during the processing of food and the instability of chemical compounds during the processing of food. The investigation sought to evaluate multilayer emulsions stabilized by ionic interfacial layers of lupin protein isolate (LPI), ι-carrageenan (CA), and chitosan (CHI) on the physical stability of the emulsion as well as the retention of astaxanthin during the spray drying process. Primary emulsion (Pr-E) was prepared by adding LPI on oil droplet surfaces containing astaxanthin. The homogenization pressure and cycles to obtain the Pr-E were investigated. The secondary emulsion (Se-E) and tertiary emulsion (Te-E) were elaborated by mixing CA/Pr-E and CHI/Se-E, respectively. Emulsion stability was assessed under different environmental stresses (pH and NaCl). Astaxanthin retention of emulsions was determined immediately after finishing the spray-drying process. The results showed that Pr-E was stabilized with 1.0% (w/v) of LPI at 50 MPa and three cycles. Se-E and Te-E were obtained with CA/Pr-E and Se-E/CHI of 70/30 and 50/50% (w/w), respectively. The Se-E was the most stable compared to the Pr-E and Te-E when subjected to different pHs; nevertheless, once the NaCl concentration rose, no variations in the ζ-potential of all emulsions studied or destabilization were observed. The Se-E and Te-E derived provided higher astaxanthin retention (>95%) during the spray-drying process compared to Pr-E (around 88%). The results indicated that these astaxanthin multilayer emulsions show considerable potential as a functional ingredient in food products.


2006 ◽  
Vol 7 (3) ◽  
pp. 453-454
Author(s):  
M. Marchesi ◽  
S. Caligari ◽  
D. Gilio ◽  
L.A. Rubio ◽  
S.K. Johnson ◽  
...  

2014 ◽  
Vol 11 (1) ◽  
pp. 9 ◽  
Author(s):  
Juliane Radtke ◽  
Stefanie Geissler ◽  
Alexandra Schutkowski ◽  
Corinna Brandsch ◽  
Holger Kluge ◽  
...  

2012 ◽  
Vol 48 (2) ◽  
pp. 568-577 ◽  
Author(s):  
Adamantini Paraskevopoulou ◽  
Andreas Chrysanthou ◽  
Maria Koutidou

2018 ◽  
Vol 135 (25) ◽  
pp. 46383 ◽  
Author(s):  
Ina Eibl ◽  
Daniela von der Haar ◽  
Marius Jesdinszki ◽  
Andreas Stäbler ◽  
Markus Schmid ◽  
...  

Foods ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 678 ◽  
Author(s):  
Katharina Schlegel ◽  
Anika Leidigkeit ◽  
Peter Eisner ◽  
Ute Schweiggert-Weisz

Lupin protein isolate was fermented with eight different microorganisms to evaluate the influence on sensory profile, techno-functional properties and protein integrity. All investigated microorganisms were able to grow in lupin protein isolate. The results showed that the foaming activity in the range of 1646–1703% and the emulsifying capacity in the range of 347–595 mL of the fermented lupin protein isolates were similar to those of the unfermented ones. Protein solubility at pH 4 showed no significant changes compared to unfermented lupin protein isolate, whereas the solubility at pH 7 decreased significantly from 63.59% for lupin protein isolate to solubilities lower than 42.35% for fermented lupin protein isolate. Fermentation with all microorganisms showed the tendency to decrease bitterness from 2.3 for lupin protein isolate (LPI) to 1.0–2.0 for the fermented ones. The most promising microorganisms for the improvement of the sensory properties of lupin protein isolates were Lactobacillus brevis as it reduced the intensity of characteristic aroma impression (pea-like, green bell pepper-like) from 4.5 to 1.0. The SDS-PAGE results showed the fermentation treatment appeared not to be sufficiently effective to destruct the protein integrity and thus, deplete the allergen potential of lupin proteins. Fermentation allows the development of food ingredients with good functional properties in foam formation and emulsifying capacity, with a well-balanced aroma and taste profile.


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