scholarly journals Stability of sunflower and rapeseed oil-in-water emulsions supplemented with ethanol-treated rapeseed meal protein isolate

2019 ◽  
Vol 56 (6) ◽  
pp. 3090-3098
Author(s):  
Hristo Kalaydzhiev ◽  
Vanya D. Gandova ◽  
Petya Ivanova ◽  
Teresa R. S. Brandão ◽  
Tzvetelin T. Dessev ◽  
...  
Keyword(s):  
Rapeseed Oil ◽  
Rapeseed Meal ◽  
Protein Isolate ◽  
Oil In Water ◽  
Meal Protein

scholarly journals Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 703
Author(s):  
Hristo Kalaydzhiev ◽  
Radoslav Georgiev ◽  
Petya Ivanova ◽  
Magdalena Stoyanova ◽  
Cristina L. M. Silva ◽  
...  
Keyword(s):  
Protein Solubility ◽  
Rapeseed Meal ◽  
Protein Isolate ◽  
Protein Fractions ◽  
Isoelectric Precipitation ◽  
Protein Isolates ◽  
Sds Page ◽  
Enhanced Solubility ◽  
Meal Protein ◽  
Biochemical Analyses

The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5–2.5 and PI2.5–8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH 10.5 to 2.5 or from pH 2.5 to 8.5, respectively. Biochemical analyses revealed that PI2.5–8.5 contained a higher amount of crude protein (72.84%) than PI10.5–2.5 (68.67%). In the same protein isolate, the level of total phenols (0.71%) was almost two-fold higher than that in PI10.5–2.5 (0.42%). No glucosinolates were established in both protein isolates. SDS-PAGE analysis demonstrated that PI10.5–2.5 contained 10 to 15 kDa protein fractions in a relatively higher amount, while PI2.5–8.5 was enriched in 18 to 29 kDa protein fractions. PI10.5–2.5 exhibited high solubility, varying from 41.74% at pH 4.5 to 65.13% at pH 6.5, while PI2.5–8.5 was almost two-fold less soluble under the same conditions. Up to pH 5.5, the addition of NaCl at 0.03 and 0.25 M diminished the solubility of PI2.5–8.5, while the solubility of PI10.5–2.5 was increased. The supplementation of PI10.5–2.5 with 0.25 M NaCl enhanced the protein solubility to 56.11% at pH 4.5 and 94.26% at pH 6.5. The addition of 0.03 M NaCl also increased the solubility of this protein isolate but to a lower extent. Overall, the approach for sequential precipitation of proteins influenced the biochemical characteristics, protein fractional profile and solubility of prepared protein isolates.

scholarly journals Identification and Capture of Phenolic Compounds from a Rapeseed Meal Protein Isolate Production Process By-Product by Macroporous Resin and Valorization Their Antioxidant Properties

Molecules ◽  
2021 ◽  
Vol 26 (19) ◽  
pp. 5853
Author(s):  
Tuong Thi Le ◽  
Xavier Framboisier ◽  
Arnaud Aymes ◽  
Armelle Ropars ◽  
Jean-Pol Frippiat ◽  
...  
Keyword(s):  
Phenolic Compounds ◽  
Antioxidant Properties ◽  
Sinapic Acid ◽  
Natural Antioxidants ◽  
Rapeseed Meal ◽  
Protein Isolate ◽  
Total Phenolic ◽  
Phenolic Contents ◽  
Meal Protein ◽  
The One

In this study, phenolic compounds from an aqueous protein by-product from rapeseed meal (RSM) were identified by HPLC-DAD and HPLC-ESI-MS, including sinapine, sinapic acid, sinapoyl glucose, and 1,2-di-sinapoyl gentibiose. The main phenolic compound in this by-product was sinapine. We also performed acid hydrolysis to convert sinapine, and sinapic acid derivatives present in the permeate, to sinapic acid. The adsorption of phenolic compounds was investigated using five macroporous resins, including XAD4, XAD7, XAD16, XAD1180, and HP20. Among them, XAD16 showed the highest total phenolic contents adsorption capacities. The adsorption behavior of phenolic compounds was described by pseudo-second-order and Langmuir models. Moreover, thermodynamics tests demonstrated that the adsorption process of phenolic compounds was exothermic and spontaneous. The highest desorption ratio was obtained with 30% (v/v) and 70% (v/v) ethanol for sinapine and sinapic acid, respectively, with a desorption ratio of 63.19 ± 0.03% and 94.68 ± 0.013%. DPPH and ABTS tests revealed that the antioxidant activity of the hydrolyzed fraction was higher than the non-hydrolyzed fraction and higher than the one of vitamin C. Antioxidant tests demonstrated that these phenolic compounds could be used as natural antioxidants, which can be applied in the food industry.

scholarly journals Effect of storage on texture and microbiological stability of o-w emulsions with inulin

2011 ◽  
Vol 29 (No. 2) ◽  
pp. 137-144 ◽  
Author(s):  
P. Glibowski ◽  
M. Kordowska-Wiater ◽  
A. Glibowska
Keyword(s):  
Shelf Life ◽  
Whey Protein ◽  
Sensory Evaluation ◽  
Rapeseed Oil ◽  
Protein Isolate ◽  
Potassium Sorbate ◽  
Oil In Water ◽  
Microbiological Stability ◽  
Polyglycerol Polyricinoleate ◽  
Intensive Growth

The aim of this study was to characterise the effect of storage at 8°C on the texture and microbiological stability of oil-in-water solid emulsions containing inulin (20% w/w) and rapeseed oil (20% w/w). The samples were analysed within 24 h from the production and after 7, 14, 28, 42, and 56 days of storage. Whey protein isolate (3% w/w) or polyglycerol polyricinoleate (1% w/w) were used as emulsifiers and half of the samples were chemically preserved with potassium sorbate (0.2% w/w). Hardness, adhesiveness, and cohesiveness did not change significantly (p≤ 0.05) during storage. Most of the samples were microbiologically stable. Only the application of the protein emulsifier had an effect on the intensive growth of microorganisms. The shelf-life of low-fat chemically preserved products based on inulin can be established to be two months. Chemical preservation of the products with non-protein emulsifiers is not necessary. Sensory evaluation of spreads containing inulin revealed a significant decrease in smoothness and meltability in the mouth and good spreadability comparable with commercial products without inulin.

Comparison of plant-based emulsifier performance in water-in-oil-in-water emulsions: Soy protein isolate, pectin and gum Arabic

2021 ◽  
Vol 307 ◽  
pp. 110625
Author(s):  
Jinning Liu ◽  
Hualu Zhou ◽  
Yunbing Tan ◽  
Jorge L. Muriel Mundo ◽  
David Julian McClements
Keyword(s):  
Soy Protein ◽  
Soy Protein Isolate ◽  
Gum Arabic ◽  
Protein Isolate ◽  
Oil In Water

scholarly journals An Escherichia coli Cell Membrane Chromatography-Offline LC-TOF-MS Method for Screening and Identifying Antimicrobial Peptides from Jatropha curcas Meal Protein Isolate Hydrolysates

2012 ◽  
Vol 17 (6) ◽  
pp. 752-760 ◽  
Author(s):  
Jianhui Xiao ◽  
Hui Zhang
Keyword(s):  
Escherichia Coli ◽  
Cell Membrane ◽  
Antimicrobial Peptides ◽  
Jatropha Curcas ◽  
High Throughput Screening ◽  
Protein Isolate ◽  
Shigella Dysenteriae ◽  
Cationic Antimicrobial Peptide ◽  
Meal Protein ◽  
Tof Ms

A novel, simple, and rapid method, named cell membrane affinity extraction (CMAE)–offline liquid chromatography time-of-flight mass spectrometry (LC-TOF-MS) was developed for screening and identifying antimicrobial peptides from Jatropha curcas meal protein isolate hydrolysates (JCMPIH) obtained by proteolytic enzyme (pepsin, trypsin, protamex, neutrase, flavourzyme, papain, alcalase, and acid protease) hydrolysis. A cationic antimicrobial peptide (CAILTHKR, JCpep8) was successfully isolated and identified by this method. Antimicrobial assay indicated that JCpep8 was active against the tested microorganisms ( Escherichia coli ATCC 25922, Shigella dysenteriae ATCC 51302, Pseudomonas aeruginosa ATCC 27553, Staphylococcus aureus ATCC 25923, Bacillus subtilis ATCC 23631, Streptococcus pneumoniae ATCC 49619) with minimal inhibitory concentration values ranging from 29 to 68 µg/mL. JCpep8 induced significant morphological alterations of the tested microbe surfaces, as shown by transmission electron microscopy, indicating strong membrane disruption. The results showed that CMAE-offline LC-TOF-MS could be a promising method for discovering high-throughput screening antimicrobial peptides from JCMPIH.

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