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

dc.citation.volume8
dc.contributor.authorLeite JAS
dc.contributor.authorMontoya CA
dc.contributor.authorLoveday SM
dc.contributor.authorMaes E
dc.contributor.authorMullaney JA
dc.contributor.authorMcNabb WC
dc.contributor.authorRoy NC
dc.contributor.editorAbd El-Aty, AM
dc.coverage.spatialSwitzerland
dc.date.accessioned2024-11-22T01:19:30Z
dc.date.available2024-11-22T01:19:30Z
dc.date.issued2021-03-10
dc.description.abstractProteases 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.
dc.description.confidentialfalse
dc.format.pagination626475-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/33777990
dc.identifier.citationLeite JAS, Montoya CA, Loveday SM, Maes E, Mullaney JA, McNabb WC, Roy NC. (2021). Heat-Treatments Affect Protease Activities and Peptide Profiles of Ruminants' Milk.. Front Nutr. 8. (pp. 626475-).
dc.identifier.doi10.3389/fnut.2021.626475
dc.identifier.eissn2296-861X
dc.identifier.elements-typejournal-article
dc.identifier.issn2296-861X
dc.identifier.numberARTN 626475
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/72054
dc.languageeng
dc.publisherFrontiers Media S.A.
dc.publisher.urihttps://www.frontiersin.org/journals/nutrition/articles/10.3389/fnut.2021.626475/full
dc.relation.isPartOfFront Nutr
dc.rights(c) 2021 The Author/s
dc.rightsCC BY 4.0
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectbovine milk
dc.subjectcaprine milk
dc.subjectcathepsin D
dc.subjectovine milk
dc.subjectpeptides
dc.subjectplasmin
dc.subjectplasminogen
dc.titleHeat-Treatments Affect Protease Activities and Peptide Profiles of Ruminants' Milk
dc.typeJournal article
pubs.elements-id443071
pubs.organisational-groupOther
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