Kinetics of immobilisation and release of tryptophan, riboflavin and peptides from whey protein microbeads

O’Neill, Graham J.; Egan, Thelma; Jacquier, Jean-Christophe; O’Sullivan, M.; O’Riordan, Dolores

doi:10.1016/j.foodchem.2015.01.131

Cited by 16 publications

(13 citation statements)

References 20 publications

(29 reference statements)

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“…Moreover, recent studies have reported successful encapsulation of dipeptide Phe-Trp and pentapeptide Leu-Trp-Met-Arg-Phe using CaCl 2 cross-linked whey protein microbeads of 1-2 mm diameter, resulting in equilibrium constants of 2.3 and 37, respectively for the peptides. 13,14 This demonstrates that the peptides are more distributed in the protein microbeads compared to the aqueous phase, with higher distribution and EE observed for the pentapeptide. Although not extensively used as carriers for peptide encapsulation, milk proteins are well established as major sources of bioactive peptides.…”

Section: Protein-based Carriersmentioning

confidence: 94%

Encapsulation of food protein hydrolysates and peptides: a review

et al. 2015

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Section: Protein-based Carriersmentioning

confidence: 94%

Encapsulation of food protein hydrolysates and peptides: a review

et al. 2015

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“…Riboflavin (RF), also known as vitamin B2, is a partially water-soluble vitamin that belongs to the group of flavoenzymes which catalyze oxidation-reduction reactions [1]. It is intrinsically fluorescent and has been used as modern drug [2]. It has been reported that RF has in vivo anti-metastatic properties in melanoma [3].…”

Section: Introductionmentioning

confidence: 99%

Albumin Submicron Particles with Entrapped Riboflavin—Fabrication and Characterization

et al. 2019

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Although riboflavin (RF) belongs to the water-soluble vitamins of group B, its solubility is low. Therefore, the application of micro-formulations may help to overcome this limiting factor for the delivery of RF. In this study we immobilized RF in newly developed albumin submicron particles prepared using the Co-precipitation Crosslinking Dissolution technique (CCD-technique) of manganese chloride and sodium carbonate in the presence of human serum albumin (HSA) and RF. The resulting RF containing HSA particles (RF-HSA-MPs) showed a narrow size distribution in the range of 0.9 to 1 μm, uniform peanut-like morphology, and a zeta-potential of −15 mV. In vitro release studies represented biphasic release profiles of RF in a phosphate buffered saline (PBS) pH 7.4 and a cell culture medium (RPMI) 1640 medium over a prolonged period. Hemolysis, platelet activation, and phagocytosis assays revealed a good hemocompatibility of RF-HSA-MPs.

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“…O′Neill et al . () demonstrated that the release kinetics of peptides encapsulated in protein micro‐beads in aqueous environment was inversely proportional to the peptide hydrophobicity. Moreover, Betancur‐Ancona et al .…”

Section: Resultsmentioning

confidence: 99%

“…The lowest values at pH 2.0 and 7.0 corresponded to the microcapsules obtained with 10 g protein 100 g À1 solid (Table 1). O 0 Neill et al (2015) demonstrated that the release kinetics of peptides encapsulated in protein microbeads in aqueous environment was inversely proportional to the peptide hydrophobicity. Moreover, Betancur-Ancona et al (2009) reported that hydrolysis with Flavourzyme Ò of P. lunatus proteins promote the generation of peptides with high surface hydrophobicity, probably due to the presence of aromatic amino acids in the sequence.…”

Section: Resultsmentioning

confidence: 99%

Bioactive Phaseolus lunatus peptides release from maltodextrin/gum arabic microcapsules obtained by spray drying after simulated gastrointestinal digestion

Cian

Campos‐Soldini

Chel‐Guerrero

et al. 2018

Int J of Food Sci Tech

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Bioactive peptides can be protected from the gastrointestinal environment by microencapsulation. The aim was to assess the effect of simulated gastrointestinal digestion on bioactive properties of P. lunatus peptides (ACE‐I, α‐glucosidase, α‐amylase, and dipeptidyl peptidase‐IV inhibition) microencapsulated by spray drying using maltodextrin/gun arabic in optimal formula. Microcapsules were formulated using a 22 factorial design. The simultaneous effect of P. lunatus hydrolysate (4 and 10 g 100 g−1) and proportion of maltodextrin/gum arabic (25:75 and 75:25 g 100 g−1) on yield, protein efficiency, size, protein release at pH 2.0 and pH 7.0 of the different microcapsules was studied. Microcapsules with maximum yield, protein efficiency, and protein release at pH 7.0, and minimum protein release at pH 2.0 were subjected to simulated gastrointestinal digestion. Microcapsules obtained in optimal formula preserved the α‐glucosidase, α‐amylase, and dipeptidyl peptidase‐IV inhibitory activity of P. lunatus peptides after in vitro gastrointestinal digestion.

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Kinetics of immobilisation and release of tryptophan, riboflavin and peptides from whey protein microbeads

Cited by 16 publications

References 20 publications

Encapsulation of food protein hydrolysates and peptides: a review

Encapsulation of food protein hydrolysates and peptides: a review

Albumin Submicron Particles with Entrapped Riboflavin—Fabrication and Characterization

Bioactive Phaseolus lunatus peptides release from maltodextrin/gum arabic microcapsules obtained by spray drying after simulated gastrointestinal digestion

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