The effect of trypsin and chymotrypsin on the in vitro antimicrobial and iron-binding properties of lactoferrin in human milk and bovine colostrumUnusual resistance of human apolactoferrin to proteolytic digestion
Abstract
The susceptibility of lactoferrin in bovine colostrum and human milk to digestion by trypsin and chymotrypsin has been investigated. Neither enzyme had much effect on the lactoferrin-mediated antimicrobial activity of human milk, and the iron binding capacity of lactoferrin in the milk was only slightly reduced. Likewise both enzymes had only a slight effect on the iron-binding capacity of purified lactoferrin. Although iron-free (apo)lactoferrin was slightly more susceptible to digestion, especially by chymotrypsin, than the iron-saturated form, the difference was much less than has been found in earlier studies with other proteins of the transferrin class. In contrast, trypsin destroyed the antimicrobial activity of bovine colostrum, and, in line with earlier studies, appreciably reduced the iron-binding capacity of both colostrum and purified bovine apolactoferrin. Bovine iron-saturated lactoferrin was more resistant to digestion. The unusual resistance of human apolactoferrin to proteolysis may reflect an evolutionary development designed to permit its survival in the gut of the infant.
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Glycans have been shown to protect immune proteins from gastrointestinal digestion so that they can retain bioactivity in the gut.
“These glycans have been shown to protect immune proteins from gastrointestinal digestion so that they can retain bioactivity in the gut [37, 38].”
From Pilot study of probiotic/colostrum supplementation on gut function in children with autism and gastrointestinal symptoms (2019) · cites this paper as [38]
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- Authors
- BRINES, R., & BROCK, J.
- Affiliations
- Western Infirmary (GB)
- Corresponding author
- BROCK, J
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 1983-09-13
- Volume
- 759
- Issue
- 3
- Pages
- 229-235
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2051521963
- Cited by
- 152
- References
- 21
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 4 · 2023: 5 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 7 · 2016: 5 · 2015: 3 · 2014: 3 · 2013: 6 · 2012: 12
- FWCI
- 1.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Infant Nutrition and Health
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Agricultural and Biological Sciences › Food Science › Animal Diversity and Health Studies
- Keywords
- lactoferrin, trypsin, chymotrypsin, proteolytic digestion, antimicrobial activity, iron-binding capacity, apo-lactoferrin, breast milk, bovine colostrum, iron-saturated lactoferrin
- MeSH terms
- Animals, Anti-Bacterial Agents, Apoproteins, Cattle, Chymotrypsin, Colostrum, Escherichia coli, Female, Humans, Iron, Kinetics, Lactoferrin, Lactoglobulins, Milk, Human, Pregnancy, Protease Inhibitors, Transferrin, Trypsin
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