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

doi:10.1016/j.foodchem.2021.130661

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

United Arab Emirates University
Universiti Sains Malaysia

Research output: Contribution to journal › Article › peer-review

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 language	English
Article number	130661
Journal	Food Chemistry
Volume	367
DOIs	https://doi.org/10.1016/j.foodchem.2021.130661
Publication status	Published - 15 Jan 2022

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

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

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10.1016/j.foodchem.2021.130661

Cite this

Mudgil, P., Baba, W. N., Kamal, H., FitzGerald, R. J., Hassan, H. M., Ayoub, M. A., Gan, C. Y., & Maqsood, S. (2022). 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. Food Chemistry, 367, Article 130661. https://doi.org/10.1016/j.foodchem.2021.130661

@article{01677d98113c42b897be562627efa265,

title = "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",

abstract = "Cow (CwC) and camel casein (CaC) hydrolysates were generated using Alcalase{\texttrademark} (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.",

keywords = "Anti-obesity, Camel casein, Cholesteryl esterase, Cow casein, Hydrolysates, Molecular interaction, Pancreatic lipase",

author = "Priti Mudgil and Baba, \{Waqas N.\} and Hina Kamal and FitzGerald, \{Richard J.\} and Hassan, \{Hassan M.\} and Ayoub, \{Mohammed Akli\} and Gan, \{Chee Yuen\} and Sajid Maqsood",

note = "Publisher Copyright: {\textcopyright} 2021 Elsevier Ltd",

year = "2022",

month = jan,

day = "15",

doi = "10.1016/j.foodchem.2021.130661",

language = "English",

volume = "367",

journal = "Food Chemistry",

issn = "0308-8146",

}

Mudgil, P, Baba, WN, Kamal, H, FitzGerald, RJ, Hassan, HM, Ayoub, MA, Gan, CY & Maqsood, S 2022, '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', Food Chemistry, vol. 367, 130661. https://doi.org/10.1016/j.foodchem.2021.130661

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. / Mudgil, Priti; Baba, Waqas N.; Kamal, Hina et al.
In: Food Chemistry, Vol. 367, 130661, 15.01.2022.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - 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

AU - Mudgil, Priti

AU - Baba, Waqas N.

AU - Kamal, Hina

AU - FitzGerald, Richard J.

AU - Hassan, Hassan M.

AU - Ayoub, Mohammed Akli

AU - Gan, Chee Yuen

AU - Maqsood, Sajid

PY - 2022/1/15

Y1 - 2022/1/15

N2 - 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.

AB - 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.

KW - Anti-obesity

KW - Camel casein

KW - Cholesteryl esterase

KW - Cow casein

KW - Hydrolysates

KW - Molecular interaction

KW - Pancreatic lipase

UR - https://www.scopus.com/pages/publications/85111578840

U2 - 10.1016/j.foodchem.2021.130661

DO - 10.1016/j.foodchem.2021.130661

M3 - Article

C2 - 34348197

AN - SCOPUS:85111578840

SN - 0308-8146

VL - 367

JO - Food Chemistry

JF - Food Chemistry

M1 - 130661

ER -

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

Abstract

UN SDGs

Keywords

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