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

Defaix, Claire; Aymes, Arnaud; Slabi, Sara Albe; Basselin, Mélody; Mathé, Christelle; Galet, Olivier; Kapel, Romain

doi:10.1016/j.foodchem.2019.01.209

Cited by 21 publications

(17 citation statements)

References 20 publications

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“…Trypsin and chymotrypsin(A) were the most effective enzyme for AMPs production (12), whereas plant proteases and subtilisin generated few AMPs (1 or 2) ( the higher number of AMPs was obtained from Cruciferin hydrolysates by trypsin and from Oleosin hydrolysates by chymotrypsin(A) (Table 4). It is known that Cruciferin accounts for about 60% of the rapeseed protein (Defaix et al, 2019). Therefore, enzymatic hydrolysis of rapeseed protein or Cruciferin using trypsin might be a promising and effective method to prepare AMPs.…”

Section: Antimicrobial Activity Prediction Of Released Peptidesmentioning

confidence: 99%

“…About 55% of rapeseed meal is produced after oil production, containing 35%-45% crude protein. Rapeseed protein mainly includes storage proteins Cruciferin, Napin, and oil body structural protein Oleosin, accounting for about 60%, 20%, and 10%, respectively (Defaix et al, 2019;Murphy et al, 1989). It has a relatively balanced amino acid (AA) composition, which makes it a high-quality plant protein resource (Ivanona et al, 2016).…”

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confidence: 99%

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Prediction and analysis of antimicrobial peptides from rapeseed protein using in silico approach

2021

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Microorganisms are one of the most important factors that affect food safety. Various chemical preservatives, such as potassium sorbate, sodium benzoate, and calcium propionate, have been used to inhibit the growth of microorganisms and prolong the shelf life of products.However, the demand of people for natural, safe, and high-quality food has been increasing. Therefore, the development of new and effective antimicrobial agents to improve food safety and extend food shelflife has attracted extensive attention. Antimicrobial peptides (AMPs) are very promising alternatives for the preservation of food products

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Section: Antimicrobial Activity Prediction Of Released Peptidesmentioning

confidence: 99%

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confidence: 99%

Prediction and analysis of antimicrobial peptides from rapeseed protein using in silico approach

2021

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“…Rapeseed protein isolate production is classically based on a solid-liquid extraction using aqueous solvents (modulated by pH and ionic strength), a clarification step, and a protein purification step. The purification is most often achieved either by tangential filtration or isoelectric precipitation [ 20 ]. Polar phenolic compounds are extracted with proteins during the extraction step and parted from proteins during the protein purification step.…”

Section: Introductionmentioning

confidence: 99%

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

Framboisier

Aymes

et al. 2021

Molecules

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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.

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“…The preparation of rapeseed protein isolate was adapted from the reported work of Defaix et al. [ 15 ] Briefly, the RPs were extracted in aqueous medium at room temperature with a solid–liquid ratio of 1:9 and 0.1 mol L −1 NaCl. pH was adjusted to 7.0 and maintained constant by adding 1 mol L −1 NaOH.…”

Section: Methodsmentioning

confidence: 99%

“…It was measured at 93.1 ± 1.5%, corresponding to an isolate grade. Protein repartition in this RP isolate was analyzed according to the methodology described by Defaix et al [15] by size-exclusion HPLC (SE-HPLC) with a column Biosep-SEC-s2000 300 × 7.8 mm, 5 µm (Phenomenex, Torrance, California, USA). It was composed of 63% globulins (M w around 300-350 kDa) and 37% albumins (M w around 10-15 kDa).…”

Section: Production Of Rp Isolatementioning

confidence: 99%

High Metal Chelating Properties from Rapeseed Meal Proteins to Counteract Lipid Oxidation in Foods: Controlled Proteolysis and Characterization

Durand

Beaubier²,

Fine

et al. 2021

Euro J Lipid Sci & Tech

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Rapeseed meal proteins (RP) are enzymatically hydrolyzed using three individual proteases (Alcalase, Flavourzyme, and Prolyve) and the enzymatic mechanism is studied. Rapeseed hydrolysates are produced under controlled conditions and the Prolyve hydrolysate is separated by membrane filtration. Their capacity to reduce free radicals (by transfer of hydrogen or electron) or transition metals (by electron transfer) in the absence of an oxidizable substrate, their metal chelating capacity as well as the antioxidant performances in model (conjugated autoxidizable triene assay) are investigated. All hydrolysates show a reduction capacity (by transfer of hydrogen or electron) and antioxidant activities, in a dose‐dependent manner, which are however not significantly increased in comparison to the native proteins. A noteworthy metal chelating activity of the peptides produced with Prolyve is highlighted. These results indicate the potential of valorization of RP as a source of high metal chelating peptides to counteract lipid oxidation in foods. Practical applications: Over the last decade, the antioxidative potential of peptides from plant biomass has been evidenced by much research. Considering the myriad of possible sources and the diversity of technology and means to obtain peptides from protein materials, it is reasonable to expect more applications. Concomitantly, preventing lipid oxidation, especially with the polyunsaturated fat‐based products, is a major concern in sectors such as agri‐food and cosmetic. Although the efficacy of synthetic antioxidants is recognized, both consumers and manufacturers are looking for more innovative, healthy, environmental‐friendly processes and quality products. In this context, a controlled proteolysis of proteins from plant by‐products can be used as a sustainable strategy to produce antioxidant peptides. Among them, new peptides released from rapeseed proteins with Prolyve can provide interesting metal chelators to counteract lipid oxidation in foods.

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

Cited by 21 publications

References 20 publications

Prediction and analysis of antimicrobial peptides from rapeseed protein using in silico approach

Prediction and analysis of antimicrobial peptides from rapeseed protein using in silico 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

High Metal Chelating Properties from Rapeseed Meal Proteins to Counteract Lipid Oxidation in Foods: Controlled Proteolysis and Characterization

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