Generation and identification of anti‐inflammatory peptides from bovine β‐casein using enzyme preparations from cod and hog

BACKGROUND: The aim of the present study was to generate and identify potential anti‐inflammatory peptides from bovine β‐casein with enzyme preparations from cod and hog. Furthermore, the potential of cod trypsin, derived from fishery by‐products, to produce these bioactive peptides for replacement...

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Bibliographic Details
Published in:Journal of the science of food and agriculture 2016-02, Vol.96 (3), p.868-877
Main Authors: Altmann, Karina, Wutkowski, Adam, Klempt, Martin, Clawin‐Rädecker, Ingrid, Meisel, Hans, Lorenzen, Peter Chr
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
anti-inflammatory activity
Anti-Inflammatory Agents - metabolism
Anti-Inflammatory Agents - pharmacology
anti-inflammatory peptides
beta-casein
Byproducts
Caseins - metabolism
Cattle
Cell Line
chymotrypsin
Chymotrypsin - metabolism
cod (fish)
enzymatic hydrolysis
enzyme activity
Enzymes
fisheries
Food-Processing Industry
Foods
Gadus morhua
Humans
Hydrolysates
Hydrolysis
identification of peptides
Industrial Waste
Ketones
Molecular Sequence Data
Peptide Fragments - chemistry
Peptide Fragments - pharmacology
Peptides
Peptides - chemistry
Peptides - metabolism
Peptides - pharmacology
Serine Endopeptidases - metabolism
Swine
Trypsin
Trypsin - metabolism
tryptic/chymotryptic enzymes
β-casein hydrolysates
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Summary:BACKGROUND: The aim of the present study was to generate and identify potential anti‐inflammatory peptides from bovine β‐casein with enzyme preparations from cod and hog. Furthermore, the potential of cod trypsin, derived from fishery by‐products, to produce these bioactive peptides for replacement of non‐food‐grade tosyl phenylalanyl chloromethyl ketone (TPCK)‐treated porcine trypsin enzyme preparation was evaluated. RESULTS: Potential anti‐inflammatory peptides were obtained by hydrolysis of β‐casein with the tryptic enzyme preparations cod trypsin, porcine trypsin (TPCK‐treated) and a porcine trypsin and chymotrypsin preparation (PTN 6.0 S). Proteolysates generated with enzyme preparations containing mainly chymotryptic activity (Cryotin, Cryotin F) did not exhibit any effect. CONCLUSION: The more chymotryptic enzyme activity is present, the lower is the potential anti‐inflammatory activity of the hydrolysates in HEKⁿᶠκᵇ ‐ ᴿᴱ cells. Comparable peptides were produced by application of porcine trypsin (TPCK) and cod trypsin. Therefore, the enzyme preparation cod trypsin can replace the non‐food‐grade porcine enzyme preparation trypsin (TPCK) for the generation of potential anti‐inflammatory peptides from β‐casein. © 2015 Society of Chemical Industry
ISSN:0022-5142
1097-0010
DOI:10.1002/jsfa.7159