Specific release of Albutensins from bovine and human serum albumin

Noni, Ivano De; Floris, René

doi:10.1016/j.idairyj.2006.06.022

Cited by 3 publications

(2 citation statements)

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“…Generation of bioactive peptides from caseins and β‐lactoglobulin has previously been studied using fermentated milk hydrolysates, which were ultrafiltrated to remove proteins followed by HPLC and identification by MS28. Other researchers have studied the release of albutensins from serum albumin after a simulated GI digest, which indicated that bioactivity of the albutensins was reduced by addition of a mixture of pancreatic enzymes30.…”

Section: Resultsmentioning

confidence: 99%

“…Using in vitro generated peptides in bioassays without further purification may be a challenge because of the remaining enzymatic activity of the added proteases, although these may be eliminated by e.g. boiling26, 30, ultrafiltration28, RP‐HPLC27, 31, or acidification or alkalinization of the digest31. Inactivation of the proteases by boiling is very efficient, but heating may induce unwanted side reactions of the peptides32, which could reduce bioactivity.…”

Section: Introductionmentioning

confidence: 99%

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Colostrum and bioactive, colostral peptides differentially modulate the innate immune response of intestinal epithelial cells

Jørgensen

Juul‐Madsen

Stagsted

2009

Journal of Peptide Science

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Characterization and identification of peptides with bioactivity from food have received considerable interest recently since such bioactive components must be adequately documented if they are part of functional food claims. We have characterized peptides from colostrum or those generated by a simulated gastrointestinal digest (GI) and tested them for bioactivity using murine intestinal (mIC(c12)) cells and compared with bioactivity of intact colostrum. The peptides were recovered in the permeate after dialysis. The presence of peptides in the permeate was confirmed by C(18) RP-HPLC, determination of free amino termini and MALDI MS. The bioactivity of the intact colostrum and colostral peptides in the permeate was tested using mIC(c12) cells stimulated in the absence or presence of different bacterial ligands that mediate cellular activation through stimulation of Toll-like receptors (TLR). Whereas intact colostrum generally reduced TLR-mediated signaling, the isolated peptides seemed to either stimulate or reduce the immune response depending on the bacterial ligand used for stimulation. Interestingly, the most potent bioactive peptides originated from nondigested colostrum, which had only been subject to endogenous protease activity. Identified peptides in the nondigested colostrum originated exclusively from the casein fraction of colostrum as shown by MALDI MS/MS identification. Thus, multiple components with different bioactivities towards the innate immune response appear in bovine colostrum.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Colostrum and bioactive, colostral peptides differentially modulate the innate immune response of intestinal epithelial cells

Jørgensen

Juul‐Madsen

Stagsted

2009

Journal of Peptide Science

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Influence of heat pre-treatment on BSA tryptic hydrolysis and peptide release

et al. 2016

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Mass Spectrometry in Protein, Peptide and Amino Acid Analysis

Corradini

Elviri

Cavazza

2010

Mass Spectrometry and Nutrition Research

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Proteins, peptides and amino acids contribute to physical properties, biological activities and sensory characteristics of foods. Proteins and peptides are widely used in formulated food due their high nutritional value and functional technological properties, such as emulsifying, gelation, foaming, and water binding. The present chapter will discuss the application of mass spectrometry-based techniques for identification and quantification of complex protein and peptide mixtures present in food matrices in order to assess food quality and safety, food authenticity, and functionality. Qualitative and quantitative MS analysis of complex food protein mixtures play a key role in understanding their nature, structure, functional and nutritional properties and impact on human health. Moreover, modern high-resolution mass spectrometry in combination with bioinformatics offers new possibilities for protein characterization, including the post-translational modifications, protein conformations and protein-protein and protein-ligand interactions.

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Specific release of Albutensins from bovine and human serum albumin

Cited by 3 publications

References 20 publications

Colostrum and bioactive, colostral peptides differentially modulate the innate immune response of intestinal epithelial cells

Colostrum and bioactive, colostral peptides differentially modulate the innate immune response of intestinal epithelial cells

Influence of heat pre-treatment on BSA tryptic hydrolysis and peptide release

Mass Spectrometry in Protein, Peptide and Amino Acid Analysis

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