Study of the in vitro digestibility of oilseed protein concentrates compared to isolates for food applications.

The research has primarily focused on isolates (>90 % protein) when studying oilseed protein products, but there is a growing interest in concentrates (65-90 % protein) due to their industrial viability and lower environmental impact. This study aimed to compare the in vitro digestibility of rapeseed and sunflower protein concentrates with isolates. Simulated digestion was conducted, and the resulting samples were analyzed using a size-exclusion chromatography approach.

Chelating peptides from rapeseed meal protein hydrolysates: identification and evaluation of their capacity to inhibit lipid oxidation.

An optimized proteolysis process was applied to rapeseed meal proteins (RP) and the hydrolysate was separated by membrane filtration allowing the production of highly metal-chelating peptides in the permeate. In order to identify the chemical structure of the most active obtained metal-chelating peptides, immobilized metal affinity chromatography (IMAC) was applied. The RP-IMAC peptide fraction was mainly composed of small peptides from 2 to 20 amino acids.

Optimization of Selective Hydrolysis of Cruciferins for Production of Potent Mineral Chelating Peptides and Napins Purification to Valorize Total Rapeseed Meal Proteins.

Preventing oxidation and microbial spoilage are both major concerns in food industries. In this context, this study aimed to valorize the total rapeseed meal proteins with controlled enzymatic proteolysis to generate potent mineral-chelating peptides from cruciferins while keeping intact the antimicrobial napins. Implementation of proteolysis of total rapeseed protein isolate with the Prolyve enzyme highlighted an interesting selective hydrolysis of the cruciferins.

Steam explosion of Aucoumea klaineana sapwood: Membrane separation of acetylated hemicelluloses.

The fractionation of the aqueous effluent of Aucoumea klaineana Pierre (Okoumé) sapwood steam explosion was examined by a sequential-dilution type membrane diafiltration. The permeate and retentate fractions were characterized by HPLC-SEC, HSQC-NMR, FTIR, UV-visible and HPAE-PAD ion chromatography. Diafiltration with 10 kDa regenerated cellulose membrane has been shown to provide efficient fractionation without fouling.

Combined Effect of Extraction and Purification Conditions on Yield, Composition and Functional and Structural Properties of Lupin Proteins.

Lupin meal presents great potential as an alternative plant-based source of proteins for human nutrition. In the present work, different conditions of extraction and purification were evaluated for production of lupin protein isolates. The results showed that the protein extraction yield was comparable at acidic and conventionally used alkaline extraction pH (37% vs.

The True Amino Acid Digestibility of 15N-Labelled Sunflower Biscuits Determined with Ileal Balance and Dual Isotope Methods in Healthy Humans.

Background: Sunflower is a promising protein source but data on amino acid (AA) digestibility are lacking in humans. Classically, the determination of AA digestibility requires ileal digesta sampling. The dual isotope method is minimally invasive but has not been compared to the conventional approach.

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

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.

Sensitization Potency of Sunflower Seed Protein in a Mouse Model: Identification of 2S-Albumins More Allergenic Than SFA-8.

Scope: Food allergy to sunflower seed (SFS) protein is not frequent and only non-specific lipid transfert protein (nsLTP) Hel a 3 is officially recognized as a food allergen. Out of the eleven seed storage 2S-albumins (SESA) detected in SFS, only SFA-8 allergenicity has been investigated so far. The study aimed then to evaluate SFS protein allergenicity and particularly, to compare the sensitization potency of SESA in a mouse model.

Production and antioxidant capacity of bioactive peptides from plant biomass to counteract lipid oxidation.

Preventing lipid oxidation, especially with the polyunsaturated fat-based products, is a major concern in sectors as agri-food and cosmetic. Even though the efficiency of synthetic antioxidants has been recognized, both consumers and manufacturers are looking for more innovative, healthy and quality products while rejecting synthetic additives due to their concern about safety, along with their environmental impact issues. In this context, plant biomass, which have shown to be rich in compounds, have raised interest for the isolation of novel naturally occurring antioxidants.

Multicriteria Optimization of Phenolic Compounds Capture from a Sunflower Protein Isolate Production Process by-Product by Adsorption Column and Assessment of Their Antioxidant and Anti-Inflammatory Effects.

The aim of this study was to valorize liquid effluent from the sunflower protein isolate process by extracting phenolic compounds it contains. To do so, XAD7 resin was used. A multicriteria optimization methodology based on design of experiments showed the optimal conditions were adsorption flow rate of 15 BV/h at pH 2.

A Rational Approach for the Production of Highly Soluble and Functional Sunflower Protein Hydrolysates.

Exploitation of plant proteins as an alternative to animal proteins currently presents an important challenge for food industries. In this contribution, total sunflower protein isolate from cold press meal was used as a starting material for the generation of highly soluble and functional hydrolysates that could be used in various food formulations. To do this, a rational and complete approach of controlled hydrolysis was implemented using the individual Alcalase and Prolyve enzymes.

Sunflower Proteins at Air-Water and Oil-Water Interfaces.

The adsorption of a sunflower protein extract at two air-water and oil-water interfaces is investigated using tensiometry, dilational viscoelasticity, and ellipsometry. For both interfaces, a three step mechanism was evidenced thanks to master curve representations of the data taken at different aging times and protein concentrations. At short times, a diffusion limited adsorption of proteins at interfaces is demonstrated.

Ultrafiltration Fractionation of Bovine Hemoglobin Hydrolysates: Prediction of Separation Performances for Optimal Enrichment in Antimicrobial Peptide.

Hydrolysis of bovine hemoglobin (bHb), the main constituent of bovine cruor by-product, releases a natural antimicrobial peptide (NKT) which could present a major interest for food safety. To enrich this, tangential ultrafiltration can be implemented, but ultrafiltration conditions are mainly empirically established. In this context, the application of a simulation method for predicting the NKT yield and enrichment was investigated.

Multi-objective optimization of solid/liquid extraction of total sunflower proteins from cold press meal.

The impact of pH (6-9) and NaCl concentration (0-0.5 mol.L) on sunflower protein extraction was studied through design of experiments.

15N and ²H Intrinsic Labeling Demonstrate That Real Digestibility in Rats of Proteins and Amino Acids from Sunflower Protein Isolate Is Almost as High as That of Goat Whey.

Background: In the context of developing plant protein sources for humans, sunflower is a good candidate in its form as an oilseed coproduct.

Objectives: We aimed to compare the real digestibility in rats of a sunflower isolate to that of goat whey protein. We also studied the efficiency of 15N and 2H intrinsic labeling in this assessment.

A new size-exclusion chromatography method for fast rapeseed albumin and globulin quantification.

The method described in the article aims at the quantification of both main storage proteins, globulins and albumins, in aqueous extract from rapeseed, as an alternative to the current reference methods, Kjeldahl and SDS-PAGE electrophoresis. The new method lies on the analytical separation of extracted compounds by Size-Exclusion High Performance Liquid Chromatography (SE-HPLC) (Biosep-SEC-s2000, 5 µm). The elution of rapeseed extracts with water/acetonitrile/trifluoroacetic acid (45/55/0.

A new SE-HPLC method for simultaneous quantification of proteins and main phenolic compounds from sunflower meal aqueous extracts.

The aim of this research was to develop a method for simultaneous quantification of proteins and main polyphenolic compounds extracted from oleaginous meal by aqueous media. Size exclusion chromatography with a Biosep column (exclusion range from 1 to 300 kDa) and acetonitrile/water/formic acid (10:89.9:0.

An aminoacylase activity from catalyzes the acylation of lysine on α-position and peptides on N-terminal position.

The presence of aminoacylase activities was investigated in a crude extract of ATCC23877. First activities catalyzing the hydrolysis of N-α or ε-acetyl-L-lysine were identified. Furthermore, the acylation of lysine and different peptides was studied and compared with results obtained with lipase B of (CALB).

Size-exclusion HPLC as a sensitive and calibrationless method for complex peptide mixtures quantification.

This work describes an original methodology to quantify complex peptide mixtures by size-exclusion high-performance liquid chromatography (SE-HPLC). The methodology was first tested on simulated elutions of peptide mixtures. For this set of experiments, a good estimation of the total peptide concentration was observed (error less than 10 %).

Recombinant pediocin in Lactococcus lactis: increased production by propeptide fusion and improved potency by co-production with PedC.

We describe the impact of two propeptides and PedC on the production yield and the potency of recombinant pediocins produced in Lactococcus lactis. On the one hand, the sequences encoding the propeptides SD or LEISSTCDA were inserted between the sequence encoding the signal peptide of Usp45 and the structural gene of the mature pediocin PA-1. On the other hand, the putative thiol-disulfide oxidoreductase PedC was coexpressed with pediocin.

Fractionation of yeast extract by nanofiltration process to assess key compounds involved in CHO cell culture improvement.

Yeast extract (YE) is known to greatly enhance mammalian cell culture performances, but its undefined composition decreases process reliability. Accordingly, in the present study, the nature of YE compounds involved in the improvement of recombinant CHO cell growth and IgG production was investigated. First, the benefits of YE were verified, revealing that it increased maximal concentrations of viable cells and IgG up to 73 and 60%, respectively compared to a reference culture.

CTAB turbidimetric method for assaying hyaluronic acid in complex environments and under cross-linked form.

The cetyltrimethylammonium bromide turbidimetric method (CTM) has been developed to quantify the hyaluronic acid (HA) in complex media to overcome the lack of selectivity and specificity of the standard carbazole method. The objective of this work is to assess the potential application of CTM to determine HA concentration. Factors such as duration of incubation, linearity range, HA size and form (natural linear HA or cross linked HA), pH and ionic environment impact were investigated.

Selective extraction, structural characterisation and antifungal activity assessment of napins from an industrial rapeseed meal.

This article reports an extraction-purification of napins from an industrial rapeseed meal and the assessment of their antimicrobial activity against Fusarium langsethiae. The best extraction conditions are observed at pH 2, 12% (w/w) of rapeseed meal after 15 min of extraction in water at room temperature. Under these conditions the extraction is highly selective, allowing a simple purification process (ammonium sulfate precipitation followed by desalting size exclusion chromatography) to get purified napins.