The food industry is focused on developing plant-based foods that incorporate pea protein isolates. However, these ingredients are often described as having persistent beany, bitter, and astringent notes, which can decrease the desirability of the resulting foods. These perceptions are rooted in the complex composition of volatile and non-volatile compounds in foods. The aim of our study was to better understand how the volatile and non-volatile fractions of pea protein isolates influence the perception of pea-protein-based foods. To this end, a mixture design was used. First, we obtained three fractions (the pellet, permeate, and retentate) from two pea protein isolates, resulting in a total of six fractions. Second, we used various combinations of the six fractions to create a set of 46 pea-protein-based solutions via various processes (solubilization, centrifugation, filtration, and mixing). Each fraction was specifically representative of the following constituent groups: insoluble proteins (the pellet); soluble compounds, such as volatiles, peptides, and phenolics (the permeate); and soluble proteins interacting with volatiles (the retentate). Factor levels were chosen with two aims: to explore the widest possible range of combinations and to realistically represent protein concentrations so as to build optimal mixture models. Third, 17 trained panelists were asked to score the attributes of the solutions using sensory profiling. Model performance was assessed using analysis of variance; results were significant for 18/18 attributes, and there was no significant lack-of-fit for 17/18 attributes. It was also assessed using the results of trials conducted with six supplementary solutions. These results clarified the origin of the perceived beany, bitter, and astringent notes. Beaniness was mainly influenced by the retentate and permeate fractions and was strongly affected by hexanal levels. Bitterness was mainly influenced by the retentate fraction, whereas astringency was influenced by the retentate and pellet fractions. Additionally, perception of these latter two attributes was affected by caffeic acid levels. This study has increased understanding of the relationship between pea protein fractions and the undesirable sensory attributes of pea protein isolates. It has also revealed how fraction-based formulation could be used to reduce the beaniness, bitterness, and astringency of pea-protein-based foods.
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http://dx.doi.org/10.1016/j.foodres.2021.110151 | DOI Listing |
The aim of this study was to use blue whiting fish protein hydrolysate (BWFPH) as a novel dietary amino acid supplement in whey protein isolate (WPI) and pea protein isolate (PPI)-based protein bars. The findings indicate that incorporating BWFPH significantly influenced the nutritional profile of the protein bars, leading to a ~93% reduction in hardness compared to bars without the hydrolysate. Additionally, BWFPH effectively delayed the hardening process during storage.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Centre of Excellence for Postharvest Biotechnology (CEPB), School of Biosciences, University of Nottingham Malaysia, Jalan Broga, Semenyih, Selangor Darul Ehsan 43500, Malaysia; Future Food Beacon of Excellence, Faculty of Science, University of Nottingham, Loughborough LE 12 5RD, United Kingdom.
Bean proteins, known for their sustainability, versatility, and high nutritional value, represent a valuable yet underutilized resource, receiving less industrial attention compared to soy and pea proteins. This review examines the structural and molecular characteristics, functional properties, amino acid composition, nutritional value, antinutritional factors, and digestibility of bean proteins. Their applications in various food systems, including baked goods, juice and milk substitutes, meat alternatives, edible coatings, and 3D printing inks, are discussed.
View Article and Find Full Text PDFSci Rep
January 2025
Center for Translational Immunology, University Medical Center Utrecht, KC 02.085.2, P.O. Box 85090, 3508 AB, Utrecht, The Netherlands.
The proximity extension assay (PEA) enables large-scale proteomic investigations across numerous proteins and samples. However, discrepancies between measurements, known as batch-effects, potentially skew downstream statistical analyses and increase the risks of false discoveries. While implementing bridging controls (BCs) on each plate has been proposed to mitigate these effects, a clear method for utilizing this strategy remains elusive.
View Article and Find Full Text PDFPoult Sci
December 2024
CBS Bio Platforms, Calgary, AB T2C 0J7, Canada.
A study was conducted to determine the effects of protease supplementation of field pea (in comparison with soybean meal; SBM) for broilers on apparent metabolizable energy (AMEn) and standardized ileal digestibility (SID) of amino acids (AA). One hundred and forty broiler chicks were divided into 35 groups of 4 birds/group and fed 5 diets in a completely randomized design (7 groups/diet) from 14 to 21 d of age. The diets were cornstarch-based containing SBM or field pea as the sole protein source without or with protease (ProSparity 250; CBS Bio Platforms, Calgary, AB, Canada) in 2 × 2 factorial arrangement, and N-free diet.
View Article and Find Full Text PDFMolecules
December 2024
Department of Inorganic Chemistry, Institute of Chemical Sciences, Faculty of Chemistry, Maria Curie-Sklodowska University in Lublin, Maria Curie-Sklodowska Sq. 3, 20-031 Lublin, Poland.
Hydrophobization could improve the moisture resistance of biopolymer-based materials, depending on the methods and materials used, providing benefits for packaging applications. The aim of this study was to compare the effect of increasing concentrations (0-2.0%) of candelilla wax (CW) and oleic acid (OA) on the structural and physicochemical properties, including water affinity, of glycerol-plasticized pea protein isolate (PPI) films.
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