Ion-pairing separation of bioactive peptides using an aqueous/octan-1-ol micro-extraction system from bovine haemoglobin complex hydrolysates

Vanhoute, M.; Froidevaux, Rénato; Vanvlassenbroeck, Aurelien; Lecouturier, Didier; Dhulster, Pascal; Guillochon, Didier

doi:10.1016/j.jchromb.2009.04.011

Cited by 7 publications

(9 citation statements)

References 30 publications

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“…This method has been proven very efficient for peptides with molar masses under 400 g/mol since in most cases (nos. [1][2][3][4][5][6][7][8][9]12) it provided the effective combination sought, which was also consistent with the sequences found in rapeseed proteins. Significant improvement in composition prediction accuracy brought by the addition of the HILIC model was illustrated by the study of peptide no.…”

Section: Application Of the Identification Strategy To A Rapeseed Prosupporting

confidence: 72%

“…When only one combination matched the first two criteria, the HILIC criterion provided confirmation of this combination which could correspond to two distinct sequences in rapeseed proteins (nos. 4,5,6,8,9). For larger peptides, the association of the three retention criteria allowed a huge drop (from 88 % for no.…”

Section: Application Of the Identification Strategy To A Rapeseed Promentioning

confidence: 99%

“…For instance, many studies reported the presence of anti-hypertensive [1][2][3][4], opioid [5,6] and antimicrobial [7][8][9] peptides in various protein hydrolysates. Furthermore, a growth-promoting [10][11][12] or growthinhibiting [13] effect in cell cultures has been reported for some protein hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

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Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

et al. 2012

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A new method to predict elementary amino acid (AA) composition of peptides (molar mass <1,000 g/mol) is described. This procedure is based on a computer-aided method using three combined analyses-reversed phase liquid chromatography (RPLC), hydrophilic interaction chromatography (HILIC) and capillary electrophoresis coupled with mass spectrometry-and using a software calculating all possible amino acid combinations from the mass of any given peptide. The complementarity between HILIC and RPLC was demonstrated. Peptide retention prediction in HILIC was successfully modelled, and the achieved prediction accuracy was as high as r²=0.97. This mathematical model, based on amino acid retention contributions and peptide length, provided the information about peptide hydrophilicity that was not redundant with its hydrophobicity. Correlations between respectively the hydrophobicity coefficients and RPLC retention time, hydrophilicity and HILIC retention time, and electrophoretic mobility and migration time were used for ranking all potential AA combinations corresponding to the given mass. The essential contribution of HILIC in this identification strategy and the need to combine the three models to significantly increase identification capabilities were both shown. Applied to an 18-standard peptide mixture, the identification procedure enabled the actual AA combination determination of the 14 di- to pentapeptides, in addition to an over 98 % reduction of possible combination numbers for the four hexapeptides. This procedure was then applied to the identification of 24 unknown peptides in a rapeseed protein hydrolysate. The effective AA composition was found for ten peptides, whereas for the 14 other peptides, the number of possible combinations was reduced by over 95 % thanks to the association of the three analyses. Finally, as a result of the information provided by the analytical techniques about peptides present in the mixture, the proposed method could become a highly valuable tool to recover bioactive peptides from undefined protein hydrolysates.

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Section: Application Of the Identification Strategy To A Rapeseed Prosupporting

confidence: 72%

Section: Application Of the Identification Strategy To A Rapeseed Promentioning

confidence: 99%

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Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

et al. 2012

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“…-Extractions using purified surfactin and fengycin were carried out using separate or mixed solutions -with and without -a protein hydrolysate from bovine collagen (Sanavita, Piracicaba, Brazil), which was added in order to lower the biosurfactant solubility by ion-pairing (Vanhoute et al 2009). In addition, a control experiment was set up using the anionic surfactant sodium dodecyl sulphate (SDS).…”

Section: Cloud Point Extraction Of P-xylenementioning

confidence: 99%

Production ofBacillus amyloliquefaciensOG and its metabolites in renewable media: valorisation for biodiesel production andp-xylene decontamination

et al. 2017

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Biosurfactants are important in many areas; however, costs impede large-scale production. This work aimed to develop a global sustainable strategy for the production of biosurfactants by a novel strain of Bacillus amyloliquefaciens. Initially, Bacillus sp. strain 0G was renamed B. amyloliquefaciens subsp. plantarum (syn. Bacillus velezensis) after analysis of the gyrA and gyrB DNA sequences. Growth in modified Landy's medium produced 3 main recoverable metabolites: surfactin, fengycin, and acetoin, which promote plant growth. Cultivation was studied in the presence of renewable carbon (as glycerol) and nitrogen (as arginine) sources. While diverse kinetics of acetoin production were observed in different media, similar yields (6-8 g·L) were obtained after 72 h of growth. Glycerol increased surfactin-specific production, while arginine increased the yields of surfactin and fengycin and increased biomass significantly. The specific production of fengycin increased ∼10 times, possibly due to a connecting pathway involving arginine and ornithine. Adding value to crude extracts and biomass, both were shown to be useful, respectively, for the removal of p-xylene from contaminated water and for biodiesel production, yielding ∼70 mg·g cells and glycerol, which could be recycled in novel media. This is the first study considering circular bioeconomy to lower the production costs of biosurfactants by valorisation of both microbial cells and their primary and secondary metabolites.

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“…Thus, ion-pairing organic solvents operating in reversedphase conditions are proven to yield highly pure peptides (Vanhoute et al 2009). Efficient recovery of biological activity is possible with most low molecular weight peptides.…”

Section: Liquid Chromatography Techniquesmentioning

confidence: 99%

Food Proteins–Peptides

Kannan¹,

Hettiarachchy²,

Marshall³

2012

Food Proteins and Peptides

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Ion-pairing separation of bioactive peptides using an aqueous/octan-1-ol micro-extraction system from bovine haemoglobin complex hydrolysates

Cited by 7 publications

References 30 publications

Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

Production ofBacillus amyloliquefaciensOG and its metabolites in renewable media: valorisation for biodiesel production andp-xylene decontamination

Food Proteins–Peptides

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