Correlation between sensory properties and peptides derived from hydrolysed-lactose UHT milk during storage

Nielsen, Søren; Jansson, Therese; Le, Thao T.; Jensen, Sidsel; Eggers, Nina; Rauh, Valentin; Sundekilde, Ulrik Kræmer; Sørensen, John Houman; Bertram, Hanne Christine; Larsen, Lotte Bach

doi:10.1016/j.idairyj.2016.12.013

Cited by 35 publications

(30 citation statements)

References 43 publications

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“…These peptidomics studies revealed that differences in starting materials, production techniques, and storage time resulted in major variation in the peptide profile. For example, peptidomics analysis of lactose-hydrolyzed ultra-high temperature heat-treated milk revealed that residual proteases in the lactase preparation caused protein degradation that led to bitter flavor development with storage time [ 166 , 167 , 168 ]. Peptidomics can also be used to monitor inter-individual divergence among cows [ 148 ] and as a tag for their health status [ 169 ].…”

Section: Advanced Analytical Techniques Of Milk and Dairy Productsmentioning

confidence: 99%

Identification and Detection of Bioactive Peptides in Milk and Dairy Products: Remarks about Agro-Foods

et al. 2020

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Food-based components represent major sources of functional bioactive compounds. Milk is a rich source of multiple bioactive peptides that not only help to fulfill consumers ‘nutritional requirements but also play a significant role in preventing several health disorders. Understanding the chemical composition of milk and its products is critical for producing consistent and high-quality dairy products and functional dairy ingredients. Over the last two decades, peptides have gained significant attention by scientific evidence for its beneficial health impacts besides their established nutrient value. Increasing awareness of essential milk proteins has facilitated the development of novel milk protein products that are progressively required for nutritional benefits. The need to better understand the beneficial effects of milk-protein derived peptides has, therefore, led to the development of analytical approaches for the isolation, separation and identification of bioactive peptides in complex dairy products. Continuous emphasis is on the biological function and nutritional characteristics of milk constituents using several powerful techniques, namely omics, model cell lines, gut microbiome analysis and imaging techniques. This review briefly describes the state-of-the-art approach of peptidomics and lipidomics profiling approaches for the identification and detection of milk-derived bioactive peptides while taking into account recent progress in their analysis and emphasizing the difficulty of analysis of these functional and endogenous peptides.

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Section: Advanced Analytical Techniques Of Milk and Dairy Productsmentioning

confidence: 99%

Identification and Detection of Bioactive Peptides in Milk and Dairy Products: Remarks about Agro-Foods

et al. 2020

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“…Peptidomics has been used to identify tumor-derived human leukocyte antigen-I (HLA-I) and HLA-II binding peptides from human tumors, which could be exploited further in precision cancer therapy [ 13 ]. It could also be used to show dairy product deterioration and to monitor the health status of cows [ 14 , 15 ]. In pigs, peptidomes have been reported in brain tissue, gastropancreatic digestion of milk proteins, plasma after hepatectomy to search for peptide indicators of liver regeneration, and epididymal sperm maturation [ 16 – 19 ].…”

Section: Discussionmentioning

confidence: 99%

Proteomic profiles of unilateral cryptorchidism in pigs at different ages using MALDI-TOF mass spectrometry and in-gel digestion coupled with mass spectrometry (GeLC-MS/MS) approaches

et al. 2020

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Background Cryptorchidism is a condition that occurs when one or both testes fail to descend into the scrotum. It is a common congenital disorder, causing economic loss in pig production. However, there have been only limited studies of differential protein expression profiles in undescended testes (UDTs) in the abdomen and descended testes (DTs) in cryptorchid pigs, especially at the peptidome and proteome levels. The present study aimed to analyze the peptidome of UDTs and DTs in unilateral cryptorchid pigs aged 1–2, 6, 15 and 20 weeks and in normal testes of healthy pigs aged 1–2 and 12 weeks, using peptide mass fingerprinting and three-dimensional principal component analysis (3D-PCA) with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, and to identify potential protein candidates, using in-gel digestion coupled with mass spectrometry (GeLC-MS/MS). Western blot analysis was used to verify protein expression. Protein sequence was affirmed by liquid chromatography–tandem mass spectrometry. Results A PCA plot showed a discrete cluster for each sample group. Peptide mass fingerprints (PMFs) demonstrated unique peptide fragments in UDTs at different ages. A number of markedly expressed proteins from GeLC-MS/MS were identified, including the multifunctional tumor necrosis factor receptor superfamily member 18 (TNFRSF18), in DTs at 1–2 and 6 weeks and in UDTs at 15 and 20 weeks of age. Using western blot analysis, high expression of TNFRSF18 was observed in the UDTs at 15 weeks. Using the STITCH database, this protein was found to be related to apoptosis, corresponding to the previous report in the UDTs at the same age. Conclusions The present study revealed the specific PMFs and clusters for porcine cryptorchidism, and a novel protein, TNFRSF18, associated with the disease mechanism. These results could provide further insights into the pathogenesis of the disease.

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“…An Agilent 1200 Series capillary HPLC system (Agilent Technologies 2000, Waldbronn, Germany), consisting of a G1376A capillary pump and a G1377A autosampler, was used together with the Agilent Chemstation software as previously described with modifications [19]. Briefly, the 10 K and 3 K filtrates of the casein hydrolysates (1 µL) were injected onto a C18 RP-HPLC column and eluted using the following elution conditions of buffer A (0.1% formic acid) and buffer B (90% acetonitrile, 0.1% formic acid): 0–5 min 2% buffer B, 5–30 min 2–100% buffer B, 30–40 min 100% buffer B.…”

Section: Methodsmentioning

confidence: 99%

Effect of Casein Hydrolysates on Intestinal Cell Migration and Their Peptide Profiles by LC-ESI/MS/MS

Nielsen

Purup

Larsen

2019

Foods

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Potential beneficial effects of bioactive peptides derived from casein on epithelial cellular wound healing in the gastrointestinal tract were studied. Bovine casein was digested by a combination of pepsin and pancreatic proteases at different time intervals to represent ranges of duration of gastrointestinal digestion. Intestinal epithelial cells were used as an in vitro model of the small intestine. The effect of casein hydrolysates on cell migration was studied by scratch assay as a model of wound healing. Casein digested by pepsin and pancreatin for 10 to 30 min were found to have a significant stimulatory effect of >40% on cell migration relative to the control. A potential effect of casein gastrointestinal digests on gastro-intestinal wound healing has not previously been reported. The peptide profiles of active as well as inactive casein hydrolysates were characterised by liquid chromatography coupled to ion trap tandem mass spectrometry. By comparison of identified peptides in active and inactive casein hydrolysates, a pool of 11 peptides derived from casein were identified as potential candidates for effects on cell migration. Searching the milk bioactive peptide database (MBPDB) showed that 15 of the identified peptides had known biological functions such as antimicrobial, antioxidant, and immunomodulatory activity.

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Correlation between sensory properties and peptides derived from hydrolysed-lactose UHT milk during storage

Cited by 35 publications

References 43 publications

Identification and Detection of Bioactive Peptides in Milk and Dairy Products: Remarks about Agro-Foods

Identification and Detection of Bioactive Peptides in Milk and Dairy Products: Remarks about Agro-Foods

Proteomic profiles of unilateral cryptorchidism in pigs at different ages using MALDI-TOF mass spectrometry and in-gel digestion coupled with mass spectrometry (GeLC-MS/MS) approaches

Effect of Casein Hydrolysates on Intestinal Cell Migration and Their Peptide Profiles by LC-ESI/MS/MS

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