In vivo endogenous proteolysis yielding beta-casein derived bioactive beta-casomorphin peptides in human breast milk for infant nutrition

Enjapoori, Ashwantha Kumar; Kukuljan, Sonja; Dwyer, Karen M.; Sharp, Julie A.

doi:10.1016/j.nut.2018.05.011

Cited by 24 publications

(13 citation statements)

References 69 publications

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“…Nonetheless, (Ferranti et al, 2004) reported in HM only the presence (not the amount) of hBCM8, despite several precursors of hBCMs were revealed. (Enjapoori et al, 2019) identified (but not quantified) hBCMs 8 to 11 in both preterm and term undigested HM samples. Precursors of hBCMs along with hBCM9 were also found by (Wada & Lönnerdal, 2015) in undigested HM without any quantitation of this peptide.…”

Section: Occurrence Of Hbcms and Bbcms In (Un)digested Pdhm And Fortimentioning

confidence: 85%

“…Other bBCMs are bBCM3 (f60-62), bBCM4 (f60-63) and bBCM6 (f60-65). Many studies reported the potential biological effect of bBCMs in adults and infants as mainly caused by interaction of bBCM7 with the μ opioid receptor (MOR) (Banks, 2015;Enjapoori, Kukuljan, Dwyer, & Sharp, 2019;Fiedorowicz et al, 2016;Kost et al, 2009). In fact, bBCMs are suspected to be involved in the onset or worsening of several non-communicable diseases (EFSA, 2009).…”

Section: Introductionmentioning

confidence: 99%

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Effect of protein fortification on heat damage and occurrence of β-casomorphins in (un)digested donor human milk intended for nutrition of preterm infants

et al. 2020

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and myself to be considered for publication in the "Food Chemistry". Highlights  Pasteurized donor human milk (PDHM) is fortified for preterm infant nutrition  Hydrolyzates of bovine milk proteins are used for fortification of PDHM  Hydrolyzates contain casomorphins (BCMs) and present protein chemical artifacts  Hydrolyzates account for the protein artifacts of PDHM  Digestion of fortified PDHM releases bovine and human BCMs *Highlights (for review)

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Section: Occurrence Of Hbcms and Bbcms In (Un)digested Pdhm And Fortimentioning

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Effect of protein fortification on heat damage and occurrence of β-casomorphins in (un)digested donor human milk intended for nutrition of preterm infants

et al. 2020

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“…The results were also used to predict the number of peptides cleaved by the main milk proteases. This approach has been used in other studies (25,33). Care is needed when interpreting the number of cleaved peptides, as it does not account for the total number of peptides in the sample.…”

Section: Discussionmentioning

confidence: 99%

Heat-Treatments Affect Protease Activities and Peptide Profiles of Ruminants' Milk

et al. 2021

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Proteases present in milk are heat-sensitive, and their activities increase or decrease depending on the intensity of the thermal treatment applied. The thermal effects on the protease activity are well-known for bovine milk but poorly understood for ovine and caprine milk. This study aimed to determine the non-specific and specific protease activities in casein and whey fractions isolated from raw bovine, ovine, and caprine milk collected in early lactation, and to determine the effects of low-temperature, long-time (63°C for 30 min) and high-temperature, short-time (85°C for 5 min) treatments on protease activities within each milk fraction. The non-specific protease activities in raw and heat-treated milk samples were determined using the substrate azocasein. Plasmin (the main protease in milk) and plasminogen-derived activities were determined using the chromogenic substrate S-2251 (D-Val-Leu-Lys-pNA dihydrochloride). Peptides were characterized using high-resolution liquid chromatography coupled with tandem mass spectrometry. The activity of all native proteases, shown as non-specific proteases, was similar between raw bovine and caprine milk samples, but lower (P < 0.05) than raw ovine milk in the whey fraction. There was no difference (P > 0.05) between the non-specific protease activity of the casein fraction of raw bovine and caprine milk samples; both had higher activity than ovine milk. After 63°C/30 min, the non-specific protease activity decreased (44%; P > 0.05) for the bovine casein fraction only. In contrast, the protease activity of the milk heated at 85°C/5 min changed depending on the species and fraction. For instance, the activity decreased by 49% for ovine whey fraction, but it increased by 68% for ovine casein fraction. Plasmin and plasminogen were in general inactivated (P > 0.05) when all milk fractions were heated at 85°C/5 min. Most of the peptides present in heat-treated milk were derived from β-casein and αS1-casein, and they matched the hydrolysis profile of cathepsin D and plasmin. Identified peptides in ruminant milk samples had purported immunomodulatory and inhibitory functions. These findings indicate that the non-specific protease activity in whey and casein fractions differed between ruminant milk species, and specific thermal treatments could be used to retain better protease activity for all ruminant milk species.

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“…Casein is present in human milk at low concentrations. Casein is not only a source of amino acids and trace elements (calcium, iron, and zinc) but also of bioactive peptides that break down and have an array of functions, including antimicrobial, gastrointestinal, immuno-modulating, and opioid activity [50][51][52]. Several peptides are formed during the proteolytic degradation of casein.…”

Section: Caseinsmentioning

confidence: 99%

“…Beta-casein (27 kDa) is the major component of the human milk casein fraction. This protein can form various bioactive peptides (phosphopeptides or opioid-like compounds) before ingestion by infants or during digestion [50]. Casein phosphopeptides (CPPs) deriving from the digestion of milk proteins have been shown to chelate calcium and facilitate its intestinal absorption, as well as other minerals like iron and zinc [34,48,52].…”

Section: Caseinsmentioning

confidence: 99%

Bioactive Compounds in Infant Formula and Their Effects on Infant Nutrition and Health: A Systematic Literature Review

Almeida

Pereira

Leandro

et al. 2021

International Journal of Food Science

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Infant formulas are an alternative to replace or supplement human milk when breastfeeding is not possible. The knowledge of human milk’s bioactive compounds and their beneficial effects has attracted the interest of researchers in the field of infant nutrition, as well as researchers of technology and food sciences that seek to improve the nutritional characteristics of infant formulas. Several scientific studies evaluate the optimization of infant formula composition. The bioactive compound inclusion has been used to upgrade the quality and nutrition of infant formulas. In this context, the purpose of this systematic literature review is to assess the scientific evidence of bioactive compounds present in infant formulas (α-lactalbumin, lactoferrin, taurine, milk fat globule membrane, folates, polyamines, long-chain polyunsaturated fatty acids, prebiotics, and probiotics) and their effects on infant nutrition and health. Through previously determined criteria, studies published in the last fifteen years from five different databases were included to identify the advances in the optimization of infant formula composition. Over the last few years, there has been optimization of the infant formula composition, not only to increase the similarities in their content of macro and micronutrients but also to include novel bioactive ingredients with potential health benefits for infants. Although the infant food industry has advanced in the last years, there is no consensus on whether novel bioactive ingredients added to infant formulas have the same functional effects as the compounds found in human milk. Thus, further studies about the impact of bioactive compounds in infant nutrition are fundamental to infant health.

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In vivo endogenous proteolysis yielding beta-casein derived bioactive beta-casomorphin peptides in human breast milk for infant nutrition

Cited by 24 publications

References 69 publications

Effect of protein fortification on heat damage and occurrence of β-casomorphins in (un)digested donor human milk intended for nutrition of preterm infants

Effect of protein fortification on heat damage and occurrence of β-casomorphins in (un)digested donor human milk intended for nutrition of preterm infants

Heat-Treatments Affect Protease Activities and Peptide Profiles of Ruminants' Milk

Bioactive Compounds in Infant Formula and Their Effects on Infant Nutrition and Health: A Systematic Literature Review

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