Proteolytic Enzymes in Human and Cow's Milk

Storrs, Arnold B.; Hull, M.E.

doi:10.3168/jds.s0022-0302(56)94824-x

Cited by 29 publications

(7 citation statements)

References 7 publications

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“…The nature of the proteolytic activity in human milk is unknown (5,20). We found proteolytic (caseinolytic) activity preferentially pattern of a,-antichymotrypsin was found in milk both with and without chymotrypsin inhibiting activity.…”

Section: Discussionmentioning

confidence: 79%

Protease Inhibitors and their Relation to Protease Activity in Human Milk

1982

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Section: Discussionmentioning

confidence: 79%

Protease Inhibitors and their Relation to Protease Activity in Human Milk

1982

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“…Greater proteolytic activity in human than in bovine milk was reported by Heegaard et al (1997), Hernell and Lonnerdal (1989) and Storrs and Hull (1956). However, Korycka-Dahl, Ribadeau Dumas, Chene, and Martal (1983) reported that the level of plasmin is about the same in human and bovine milk, but that the former contains about four times more plasminogen.…”

Section: Human Milkmentioning

confidence: 83%

Indigenous enzymes in milk: Overview and historical aspects—Part 1

Fox

Kelly

2006

International Dairy Journal

184

134

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“…100 μL of human milk was spread over the surface of skim milk agar and incubated at 37°C for 24 to 48 hours. Proteolytic bacteria were indicated by clean zones around the colonies (Storrs & Hull, 1956).…”

Section: Methodsmentioning

confidence: 99%

Peptidomic profiling of human milk with LC–MS/MS reveals pH-specific proteolysis of milk proteins

et al. 2019

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Human milk is a dynamic protein-protease system that delivers bioactive peptides to infants. The pH of milk changes from the mother’s mammary gland to the infant’s digestive tract. Although the release of human milk peptides has been studied during in vivo or in vitro digestion, these models did not explicitly vary nor observe the effect of pH. The objective of this research was to determine the effect of pH on the proteolysis of human milk. Using high-resolution accurate-mass Orbitrap mass spectrometry, profiles of endogenous human milk peptides before and after incubation at various pH levels have been mapped. Over 5000 peptides were identified. Comparative analyses classified 74 peptides that were consistently found independent of pH alterations, and 8 peptides that were released only at pH 4 or 5 (typical infant gastric pH). Results documented that the proteolysis of milk proteins, particularly β-casein, polymeric immunoglobulin receptor, and α-lactalbumin, is pH-dependent.

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Proteolytic Enzymes in Human and Cow's Milk

Cited by 29 publications

References 7 publications

Protease Inhibitors and their Relation to Protease Activity in Human Milk

Protease Inhibitors and their Relation to Protease Activity in Human Milk

Indigenous enzymes in milk: Overview and historical aspects—Part 1

Peptidomic profiling of human milk with LC–MS/MS reveals pH-specific proteolysis of milk proteins

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