Optimization of a Pilot-Scale Process for Producing Lupin Protein Isolates with Valuable Technological Properties and Minimum Thermal Damage

2006 ◽  
Vol 54 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Alessandra D'Agostina ◽  
Cristina Antonioni ◽  
Donatella Resta ◽  
Anna Arnoldi ◽  
Jürgen Bez ◽  
...  
Keyword(s):  
Thermal Damage ◽  
Pilot Scale ◽  
Technological Properties ◽  
Protein Isolates ◽  
Lupin Protein

Functional Properties of Lupin Protein Isolates (Lupinus albus cv Multolupa)

2006 ◽  
Vol 50 (1) ◽  
pp. 82-87 ◽  
Author(s):  
J. KING ◽  
C. AGUIRRE ◽  
S. De PABLO
Keyword(s):  
Functional Properties ◽  
Lupinus Albus ◽  
Protein Isolates ◽  
Lupin Protein

scholarly journals Techno-Functional, Nutritional and Environmental Performance of Protein Isolates from Blue Lupin and White Lupin

Foods ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 230 ◽  
Author(s):  
Martin Vogelsang-O’Dwyer ◽  
Juergen Bez ◽  
Iben Lykke Petersen ◽  
Marcel Skejovic Joehnke ◽  
Andreas Detzel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Environmental Impacts ◽  
Milk Powder ◽  
Protein Isolate ◽  
White Lupin ◽  
Trypsin Inhibitor Activity ◽  
Foaming Properties ◽  
Protein Isolates ◽  
Lupin Protein

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.

Technological properties and non-enzymatic browning of white lupin protein enriched spaghetti

2007 ◽  
Vol 101 (1) ◽  
pp. 57-64 ◽  
Author(s):  
Georgios Doxastakis ◽  
Maria Papageorgiou ◽  
Dimitra Mandalou ◽  
Maria Irakli ◽  
Evdoxia Papalamprou ◽  
...  
Keyword(s):  
White Lupin ◽  
Enzymatic Browning ◽  
Technological Properties ◽  
Lupin Protein

Foaming activity of lupin protein isolates in the absence of insoluble protein aggregates

2011 ◽  
Vol 382 (1-3) ◽  
pp. 74-80 ◽  
Author(s):  
T.D. Karapantsios ◽  
V.T. Papoti ◽  
G. Doxastakis
Keyword(s):  
Protein Aggregates ◽  
Insoluble Protein ◽  
Protein Isolates ◽  
Lupin Protein

scholarly journals Enzymatic hydrolysis of lupin protein isolates—Changes in the molecular weight distribution, technofunctional characteristics, and sensory attributes

2019 ◽  
Vol 7 (8) ◽  
pp. 2747-2759 ◽  
Author(s):  
Katharina Schlegel ◽  
Katharina Sontheimer ◽  
Andrea Hickisch ◽  
Ali Abas Wani ◽  
Peter Eisner ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Enzymatic Hydrolysis ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Sensory Attributes ◽  
Protein Isolates ◽  
Lupin Protein ◽  
Hydrolysis Of

scholarly journals Technofunctional and Sensory Properties of Fermented Lupin Protein Isolates

Foods ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 678 ◽  
Author(s):  
Katharina Schlegel ◽  
Anika Leidigkeit ◽  
Peter Eisner ◽  
Ute Schweiggert-Weisz
Keyword(s):  
Functional Properties ◽  
Lactobacillus Brevis ◽  
Protein Isolate ◽  
Sensory Properties ◽  
Sensory Profile ◽  
Foam Formation ◽  
Food Ingredients ◽  
Protein Isolates ◽  
Lupin Protein ◽  
Emulsifying Capacity

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.

Pilot scale preparation of wheat gluten protein fractions: II. Technological properties of the fractions

1996 ◽  
Vol 31 (1) ◽  
pp. 77-83 ◽  
Author(s):  
Serge Berot ◽  
Hubert Chiron ◽  
Michel Nicolas ◽  
Sylvie Gautier ◽  
Bernard Godon ◽  
...  
Keyword(s):  
Wheat Gluten ◽  
Pilot Scale ◽  
Protein Fractions ◽  
Gluten Protein ◽  
Technological Properties ◽  
Scale Preparation

scholarly journals Contribution of S. xylosus and L. sakei ssp. carnosus Fermentation to the Aroma of Lupin Protein Isolates

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1257
Author(s):  
Katharina Schlegel ◽  
Eva Ortner ◽  
Andrea Buettner ◽  
Ute Schweiggert-Weisz
Keyword(s):  
Protein Isolate ◽  
Gas Chromatography Mass Spectrometry ◽  
Lactobacillus Sakei ◽  
Butanoic Acid ◽  
Active Compounds ◽  
Protein Isolates ◽  
Aroma Profile ◽  
Stable Isotope Dilution ◽  
Staphylococcus Xylosus ◽  
Lupin Protein

Aroma-active compounds of lupin protein isolate and lupin protein isolate fermented with Staphylococcus xylosus and Lactobacillus sakei ssp. carnosus were investigated. The changes in aroma-active compounds were determined by application of aroma extract dilution analysis in combination with gas chromatography-mass spectrometry/olfactometry for identification, and by stable isotope dilution assays for quantification. A total of 30 aroma-active compounds for non-fermented and fermented samples were identified. The aroma profile of LPI fermented with Lactobacillus sakei ssp. carnosus was characterized as roasty and popcorn-like. Staphylococcus xylosus generated cheesy impressions, being in line with the fact that the main aroma compounds acetic acid, butanoic acid, and 2/3-methylbutanoic acid could be identified. Quantification of butanoic acid further confirmed these findings with the highest concentration of 140 mg/kg for LPI fermented with Staphylococcus xylosus. Our study provides insights into how fermentation utilizing different fermentative microbial strains, namely Staphylococcus xylosus and Lactobacillus sakei ssp. carnosus alters the aroma profile of lupin protein isolates. This demonstrates the potential of shaping fermented protein-based foods via targeted microbiological refinement.

New processing of lupin protein isolates and functional properties

Nahrung/Food ◽  
2001 ◽  
Vol 45 (6) ◽  
pp. 393 ◽  
Author(s):  
A. Wäsche ◽  
K. Müller ◽  
U. Knauf
Keyword(s):  
Functional Properties ◽  
Protein Isolates ◽  
Lupin Protein ◽  
New Processing

In vitro binding of bile acids by lupin protein isolates and their hydrolysates

2004 ◽  
Vol 88 (2) ◽  
pp. 179-184 ◽  
Author(s):  
Yumiko Yoshie-Stark ◽  
Andreas Wäsche
Keyword(s):  
Bile Acids ◽  
Protein Isolates ◽  
In Vitro Binding ◽  
Lupin Protein ◽  
Vitro Binding
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