A comparative investigation into novel cholesterol esterase and pancreatic lipase inhibitory peptides from cow and camel casein hydrolysates generated upon enzymatic hydrolysis and in-vitro digestion

Priti Mudgil, Waqas N. Baba, Hina Kamal, Richard J. FitzGerald, Hassan M. Hassan, Mohammed Akli Ayoub, Chee Yuen Gan, Sajid Maqsood

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

Cow (CwC) and camel casein (CaC) hydrolysates were generated using Alcalase™ (CwCA and CaCA) and Pronase-E (CwCP and CaCP) each for 3 and 6 h, and investigated for their potential to inhibit key lipid digesting enzymes i.e., pancreatic lipase (PL) and cholesteryl esterase (CE). Results revealed stronger PL and CE inhibition by CaC hydrolysates compared to CwC. Potent hydrolysates (CwCP-3 h and CaCA-6 h) upon simulated gastrointestinal digestion (SGID) showed significant improvement in inhibition of both PL and CE. However, both the SGID hydrolysates showed similar extent of PL and CE inhibition and were further sequenced for peptide identification. Peptides MMML, FDML, HLPGRG from CwC and AAGF, MSNYF, FLWPEYGAL from CaC hydrolysates were predicted to be most active PL inhibitory peptides. Peptide LP found in both CwC and CaC hydrolysates was predicted as active CE inhibitor. Thus, CwC and CaC could be potential source of peptides with promising CE and PL inhibitory properties.

Original languageBritish English
Article number130661
JournalFood Chemistry
Volume367
DOIs
StatePublished - 15 Jan 2022

Keywords

  • Anti-obesity
  • Camel casein
  • Cholesteryl esterase
  • Cow casein
  • Hydrolysates
  • Molecular interaction
  • Pancreatic lipase

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