Immunomodulatory activity of protein hydrolysates derived from Virgibacillus halodenitrificans SK1-3-7 proteinase.
Modulation of inflammation-related immune response on THP-1 macrophages of protein hydrolysates derived from tilapia mince, casein and pea protein, were investigated. The protein substrates were hydrolyzed by Virgibacillus halodenitrificans SK1-3-7 proteinase. The degree of hydrolysis (DH) of casein was observed to be the highest throughout the course of hydrolysis. When challenging THP-1 macrophages, tilapia mince hydrolysate (TMH) enhanced innate immunity through induction of IL-1β and COX-2 expression. Anti-inflammatory activity was observed in casein hydrolysate (CH) and pea protein hydrolysate (PPH) by attenuating lipopolysaccharide- (LPS) induced pro-inflammatory gene expression in THP-1 macrophages. CH suppressed IL-1β, IL-6, IL-8, TNF-α and COX-2, while PPH reduced LPS-induced IL-6 and TNF-α responses. In addition, CH and PPH showed stronger suppression of LPS-induced pro-inflammatory gene expression compared with non-hydrolyzed casein and pea protein. These results suggest that TMH, CH and PPH prepared from V. halodenitrificans SK1-3-7 proteinase are potential functional food ingredients with immunomodulatory activity.
School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
Tidarat
T
Toopcham
Food & Biobased Research, Wageningen University and Research Centre, Bornse Weilanden 9, P.O. Box 17, 6700 AA Wageningen, The Netherlands.
Jurriaan J
JJ
Mes
Food & Biobased Research, Wageningen University and Research Centre, Bornse Weilanden 9, P.O. Box 17, 6700 AA Wageningen, The Netherlands. Electronic address: harry.wichers@wur.nl.
Harry J
HJ
Wichers
School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand. Electronic address: jirawat@sut.ac.th.
Jirawat
J
Yongsawatdigul
D000818:Animals; D000893:Anti-Inflammatory Agents / Q000494:pharmacology; D002364:Caseins / Q000494:pharmacology*; D002478:Cells, Cultured; D023681:Cichlids; D051546:Cyclooxygenase 2 / Q000235:genetics / Q000378:metabolism; D029941:Fish Proteins / Q000494:pharmacology*; D005786:Gene Expression Regulation; D006801:Humans; D006868:Hydrolysis; D007113:Immunity, Innate; D056747:Immunomodulation; D007249:Inflammation; D053583:Interleukin-1beta / Q000235:genetics / Q000378:metabolism; D015850:Interleukin-6 / Q000235:genetics / Q000378:metabolism; D016209:Interleukin-8 / Q000235:genetics / Q000378:metabolism; D008070:Lipopolysaccharides / Q000633:toxicity; D008264:Macrophages / Q000187:drug effects / Q000378:metabolism; D018532:Pisum sativum / Q000737:chemistry; D010447:Peptide Hydrolases / Q000378:metabolism*; D010940:Plant Proteins / Q000494:pharmacology; D011492:Protein Hydrolysates / Q000494:pharmacology*; D014409:Tumor Necrosis Factor-alpha / Q000235:genetics / Q000378:metabolism; D058679:Virgibacillus / Q000201:enzymology*
D000893:Anti-Inflammatory Agents; D002364:Caseins; D029941:Fish Proteins; D053583:Interleukin-1beta; D015850:Interleukin-6; D016209:Interleukin-8; D008070:Lipopolysaccharides; D010940:Plant Proteins; D011492:Protein Hydrolysates; D014409:Tumor Necrosis Factor-alpha; C475729:casein hydrolysate; D051546:Cyclooxygenase 2; D010447:Peptide Hydrolases
Immunomodulation; Inflammation; Macrophages; Protein hydrolysate