TY - JOUR
T1 - Identification and molecular mechanisms of novel antioxidative peptides from fermented camel milk (Kachchi breed, India) with anti-inflammatory activity in raw macrophages cell lines
AU - Dharmisthaben, Patel
AU - Sakure, Amar
AU - Liu, Zhenbin
AU - Maurya, Ruchika
AU - Das, Sujit
AU - Basaiawmoit, Bethsheba
AU - Kumari, Reena
AU - Bishnoi, Mahendra
AU - Kondepudi, Kanthi Kiran
AU - Gawai, Kunal M.
AU - Baba, Waqas N.
AU - Maqsood, Sajid
AU - Hati, Subrota
N1 - Publisher Copyright:
© 2022 Society of Dairy Technology.
PY - 2023/2
Y1 - 2023/2
N2 - The investigation was aimed at assessing anti-inflammatory and antioxidative activities along with the release of peptides with antioxidative properties during the fermentation of camel milk by Lacticaseibacillus casei (NK9). Reverse-phase high-performance liquid chromatography (RP-HPLC) was used to separate the bioactive peptides of 3 and 10 kDa (permeates and retentates). Reverse-phase liquid chromatography–mass spectrometry (RPLC/MS) was used to identify and characterise the pure bioactive peptides, and the effect of fermented camel milk on inflammation produced by lipopolysaccharide (LPS)/endotoxin in RAW 264.7 (Ralph and William's cell line) was also examined. Furthermore, docking revealed that peptides (LLNEK and IYTFPQPQSL) were predicted to inhibit myeloperoxidase (nMPO) activity by engaging with different residues in and around the human myeloperoxidase (hMPO) active site.
AB - The investigation was aimed at assessing anti-inflammatory and antioxidative activities along with the release of peptides with antioxidative properties during the fermentation of camel milk by Lacticaseibacillus casei (NK9). Reverse-phase high-performance liquid chromatography (RP-HPLC) was used to separate the bioactive peptides of 3 and 10 kDa (permeates and retentates). Reverse-phase liquid chromatography–mass spectrometry (RPLC/MS) was used to identify and characterise the pure bioactive peptides, and the effect of fermented camel milk on inflammation produced by lipopolysaccharide (LPS)/endotoxin in RAW 264.7 (Ralph and William's cell line) was also examined. Furthermore, docking revealed that peptides (LLNEK and IYTFPQPQSL) were predicted to inhibit myeloperoxidase (nMPO) activity by engaging with different residues in and around the human myeloperoxidase (hMPO) active site.
KW - Anti-inflammatory
KW - Antioxidant activity
KW - Antioxidative peptides
KW - Fermented camel milk (FCM)
KW - Lacticaseibacillus casei
KW - Molecular docking
KW - Proteolytic activity
UR - http://www.scopus.com/inward/record.url?scp=85140028448&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85140028448&partnerID=8YFLogxK
U2 - 10.1111/1471-0307.12911
DO - 10.1111/1471-0307.12911
M3 - Article
AN - SCOPUS:85140028448
SN - 1364-727X
VL - 76
SP - 111
EP - 125
JO - International Journal of Dairy Technology
JF - International Journal of Dairy Technology
IS - 1
ER -