scholarly journals Quality Attributes of Ultra-High Temperature-Treated Model Beverages Prepared with Faba Bean Protein Concentrates

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1244
Author(s):  
Malik Adil Nawaz ◽  
Tanoj Kumar Singh ◽  
Regine Stockmann ◽  
Hema Jegasothy ◽  
Roman Buckow

The objective of this research was to develop a model faba bean drink with a high concentration of protein (>4% w/w). The protein molecular weights and frequency for both faba and soy were assessed using SDS-PAGE. Results showed similarities in the protein molecular weight of both faba and soy (mainly 11S globulin ~Glycinin and 7S globulin ~β-conglycinin). Thus, faba can be considered as a potential soy replica in plant-based milk beverages. Oil-in-water emulsions (5–8% w/w available protein) were prepared using faba bean protein concentrate (FPC), 1% sunflower oil, and 0.2% sunflower lecithin. These emulsions were used as model beverages and were further investigated for UHT processibility, stability, and physicochemical properties. The physicochemical properties of emulsions at various processing stages viz., coarse emulsification, homogenisation, and UHT, were measured. An increase in the protein concentration and thermal treatment resulted in an increased oil droplet size, coalescence and flocculation, and protein aggregation. Lower protein concentrations viz., 5–6%, showed greater negative ζ-potential, and thereby, high dispersibility through enhanced electrostatic repulsions than those of higher concentrations (7–8%). Furthermore, an increase in protein concentration and UHT treatment resulted in an increased creaming index. In total, 21 different volatile compounds were detected and quantified, representing different chemical classes, namely alcohols, aldehydes, ketones, esters, furan, and acids. These volatiles have major consequences for the overall flavour chemistry of the model beverage product. Overall, this study showed the potential for application of faba bean as a protein source in UHT-treated legume-based beverages and identified areas for further development.

Proceedings ◽  
2020 ◽  
Vol 70 (1) ◽  
pp. 29
Author(s):  
Malik Adil Nawaz ◽  
Tanoj Kumar Singh ◽  
Hema Jegasothy ◽  
Roman Buckow

Faba beans are one of the most consumed legumes and an emerging source of edible legume-based protein. Efficacy of faba bean protein concentrate (available protein ~ 63%) during ultra-heat treatment (UHT) processing of homogenised oil-in-water (O/W) emulsion was assessed in the present study by using four different concentrations viz., FPC5 ~ 5%, FPC6 ~ 6%, FPC7 ~ 7%, and FPC8 ~ 8%. Additionally, the physicochemical properties of emulsion at various processing stages viz., coarse, homogenised, and UHT were also measured. Overall, this study showed the potential use of faba bean protein as a replica of soy protein in UHT processed legume-based beverages.


1995 ◽  
Vol 62 (3) ◽  
pp. 431-439 ◽  
Author(s):  
Joanna R. Brown ◽  
Andrew J. R. Law ◽  
Christopher H. Knight

SummaryFive British Saanen goats were milk sampled during the first 39 weeks of lactation to determine changes in casein composition. Caseins were separated by anion- and cation-exchange FPLC to determine the relative amounts of the individual caseins. Acid, alkaline and SDS-PAGE were used to determine possible genetic polymorphisms and observe any lactational changes. Total casein nitrogen was determined using a micro-Kjeldahl method and this allowed the concentrations of individual caseins to be calculated. The milk of one animal, which had the deduced genotype αs1-CnAB, showed higher concentrations of both total and αs1-casein. The remainder of the group were either heterozygous αs1-CnBE or, more probably, homozygous αs1-CnE and produced milk of a generally lower protein concentration. Both FPLC and PAGE results showed that the relative amounts and concentrations of αs2-casein decreased with stage of lactation, consistent with its susceptibility to proteolysis. The relative amounts of the breakdown products of plasmin attack on β-casein, γ-caseins, were highly negatively correlated with milk yield (r = –0·942, P < 0·001) in the declining phase of lactation, reflecting the gradual involution of the gland at this time. The relative amount of κ-casein increased by ∼ 50% after peak lactation and its concentration almost doubled near the end of lactation. These compositional changes may alter the processing qualities of goats' milk in relation to cheese production.


1979 ◽  
Vol 42 (04) ◽  
pp. 1306-1315 ◽  
Author(s):  
Janet L Lane ◽  
H Ekert ◽  
A Vafiadis

SummaryFactor VIII, purified by gel filtration on Sepharose 2B, has an 8 band multiple subunit structure, with molecular weights ranging from 30,000 to 230,000, on reduction and SDS-PAGE at a protein concentration of 400 μg/gel. Affinity chromatography of this factor VIII preparation with insolubilized haemophilic antibody to factor VIII showed that 45-81% VIII:C and 0-33% VIILRag were attached to the column. Elution of the column with 0.25 M CaCl2 did not show VIII:C or VIILRag in the eluate. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the dissociated protein, showed that 95 % of the protein bound by haemophilic antibody had a molecular weight similar to the low molecular weight subunits of the reduced factor VIII.In control experiments with normal Human IgG, 3% of VIII:C and 5% of VIILRag were attached to the column. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the protein, showed 2 faint bands with molecular weight consistent with heavy and light chains of IgG.Similar experiments with antibody to factor VIII showed that 67-83% of VIILC and 61-76% of VIII:Rag were attached to the column. Elution of the column with 0.25 M CaCl2 showed 10% of the applied VIII:C, but no VIII:Rag in the eluate. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the dissociated protein, showed an 8 band subunit structure similar to the reduced factor VIII.


2021 ◽  
Vol 49 (2) ◽  
pp. 202-211
Author(s):  
Marcelo U. García-Guerrero ◽  
Dulce M. Mateos-Guerrero ◽  
Juan J. Alpuche-Osorno ◽  
Rodolfo B. De los Santos-Romero

A good understanding of a given species' embryology is important to settle the larval rearing bases when juveniles are required for culture purposes or conservation programs. Changes in embryonic morphology, protein concentration, and protein type occurring in prawn eggs were analyzed in the present work. Berried females of Macrobrachium tenellum were collected in the Colotepec River, Oaxaca, Mexico. The eggs were taken from the ovigerous mass and embryonic stages classified by their color. Morphological changes in the embryos allowed identifying six embryonic stages based on color, egg size, and morphological features. Determinations of the protein extract were executed in SDS-PAGE (electrophoresis in polyacrylamide gels) and, subsequently, proteomic analyses were also performed. Protein bands along embryonic development and their molecular weights are presented and commented.


OENO One ◽  
1996 ◽  
Vol 30 (2) ◽  
pp. 103
Author(s):  
Laurent Berthier ◽  
Richard Marchal ◽  
Alain Maujean

<p style="text-align: justify;">In order ta estimate c1arifying aptitude and the effects of prefermentation treatment by commercial pectinases, polygalacturonase (PG), pectin Iyase (PL), pectinmethylesterase (PME) and proteolytic activities of six pectinases samples were studied. PG activity is preponderate and proportional to the relative protein concentration.</p><p style="text-align: justify;">These one, submitted to both SDS-PAGE and isoelectric focusing technics, show molecular weights ranging from 20 ta 100 kDa and isoelectric points ranging from 3.00 ta 7.40. Total protein of Champagne grape varieties Chardonnay (CH) and Pinot noir (PN) - were submitted to an isoelectric focusing. All of the pI's ranging from 3.30 to 4.55 (CH) and from 3.30 to 4.90 (PN). Proteases are put in evidence in commercial pectinases using fluorescamine- casein as substrate. However, they seem to have no incidence upon must proteins.</p>


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