Simulated gastrointestinal digestion of camel and bovine casein hydrolysates: Identification and characterization of novel anti-diabetic bioactive peptides

Priti Mudgil; Hina Kamal; Bhanu Priya Kilari; Mohd Adam Salim Mohd Salim; Chee Yuen Gan; Sajid Maqsood

doi:10.1016/j.foodchem.2021.129374

Simulated gastrointestinal digestion of camel and bovine casein hydrolysates: Identification and characterization of novel anti-diabetic bioactive peptides

Priti Mudgil, Hina Kamal, Bhanu Priya Kilari, Mohd Adam Salim Mohd Salim, Chee Yuen Gan, Sajid Maqsood

Department of Food, Nutrition and Health

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

45 Citations (Scopus)

Abstract

Camel milk proteins are an important substrate for bioactive peptides generation. This study investigates in-vitro antidiabetic effect (via inhibition of α-amylase (AA), α-glucosidase (AG) and dipeptidyl peptidase IV (DPP-IV)) of bovine (BC) and camel casein (CC) hydrolysates. Further, effect of simulated gastrointestinal digestion (SGID) on inhibitory potential of generated hydrolysates was also explored. Both BC and CC hydrolysates displayed potent inhibitory properties against AA (IC₅₀ value- 0.58 & 0.59 mg/mL), AG (IC₅₀ value- 1.04 & 0.59 mg/mL) and DPP-IV (IC₅₀ value- 0.62 & 0.66 mg/mL), respectively. Among different peptides identified in BC and CC hydrolysates, it was observed that FLWPEYGAL was predicted to be most potent inhibitory peptide against AA. While LPTGWLM, MFE and GPAHCLL as most active inhibitor of AG and HLPGRG, QNVLPLH and PLMLP were predicted to be active against DPP-IV. Overall, BC and CC hydrolysates can be proposed to be used in different food formulations as functional antidiabetic agents.

Original language	English
Article number	129374
Journal	Food Chemistry
Volume	353
DOIs	https://doi.org/10.1016/j.foodchem.2021.129374
Publication status	Published - Aug 15 2021

Keywords

Anti-diabetic
Bovine casein
Camel casein
Dipeptidyl peptidase-IV (DPP-IV)
Peptide sequencing
Protein hydrolysates
α-Amylase (AA)
α-Glucosidase (AG)

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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10.1016/j.foodchem.2021.129374

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title = "Simulated gastrointestinal digestion of camel and bovine casein hydrolysates: Identification and characterization of novel anti-diabetic bioactive peptides",

abstract = "Camel milk proteins are an important substrate for bioactive peptides generation. This study investigates in-vitro antidiabetic effect (via inhibition of α-amylase (AA), α-glucosidase (AG) and dipeptidyl peptidase IV (DPP-IV)) of bovine (BC) and camel casein (CC) hydrolysates. Further, effect of simulated gastrointestinal digestion (SGID) on inhibitory potential of generated hydrolysates was also explored. Both BC and CC hydrolysates displayed potent inhibitory properties against AA (IC50 value- 0.58 & 0.59 mg/mL), AG (IC50 value- 1.04 & 0.59 mg/mL) and DPP-IV (IC50 value- 0.62 & 0.66 mg/mL), respectively. Among different peptides identified in BC and CC hydrolysates, it was observed that FLWPEYGAL was predicted to be most potent inhibitory peptide against AA. While LPTGWLM, MFE and GPAHCLL as most active inhibitor of AG and HLPGRG, QNVLPLH and PLMLP were predicted to be active against DPP-IV. Overall, BC and CC hydrolysates can be proposed to be used in different food formulations as functional antidiabetic agents.",

keywords = "Anti-diabetic, Bovine casein, Camel casein, Dipeptidyl peptidase-IV (DPP-IV), Peptide sequencing, Protein hydrolysates, α-Amylase (AA), α-Glucosidase (AG)",

author = "Priti Mudgil and Hina Kamal and {Priya Kilari}, Bhanu and {Mohd Salim}, {Mohd Adam Salim} and Gan, {Chee Yuen} and Sajid Maqsood",

note = "Funding Information: Authors are thankful to United Arab Emirates University for funding this research through a research grants (UPAR-31F094) awarded to PI, Sajid Maqsood. University Sains Malaysia RUI grant (1001/CABR/8011045) to Chee-Yuen Gan is also acknowledged. Dr. Hassan. M. Hassan is acknowledged for RP-UPLC analysis. Publisher Copyright: {\textcopyright} 2021 Elsevier Ltd",

year = "2021",

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doi = "10.1016/j.foodchem.2021.129374",

language = "English",

volume = "353",

journal = "Food Chemistry",

issn = "0308-8146",

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TY - JOUR

T1 - Simulated gastrointestinal digestion of camel and bovine casein hydrolysates

T2 - Identification and characterization of novel anti-diabetic bioactive peptides

AU - Mudgil, Priti

AU - Kamal, Hina

AU - Priya Kilari, Bhanu

AU - Mohd Salim, Mohd Adam Salim

AU - Gan, Chee Yuen

AU - Maqsood, Sajid

N1 - Funding Information: Authors are thankful to United Arab Emirates University for funding this research through a research grants (UPAR-31F094) awarded to PI, Sajid Maqsood. University Sains Malaysia RUI grant (1001/CABR/8011045) to Chee-Yuen Gan is also acknowledged. Dr. Hassan. M. Hassan is acknowledged for RP-UPLC analysis. Publisher Copyright: © 2021 Elsevier Ltd

PY - 2021/8/15

Y1 - 2021/8/15

N2 - Camel milk proteins are an important substrate for bioactive peptides generation. This study investigates in-vitro antidiabetic effect (via inhibition of α-amylase (AA), α-glucosidase (AG) and dipeptidyl peptidase IV (DPP-IV)) of bovine (BC) and camel casein (CC) hydrolysates. Further, effect of simulated gastrointestinal digestion (SGID) on inhibitory potential of generated hydrolysates was also explored. Both BC and CC hydrolysates displayed potent inhibitory properties against AA (IC50 value- 0.58 & 0.59 mg/mL), AG (IC50 value- 1.04 & 0.59 mg/mL) and DPP-IV (IC50 value- 0.62 & 0.66 mg/mL), respectively. Among different peptides identified in BC and CC hydrolysates, it was observed that FLWPEYGAL was predicted to be most potent inhibitory peptide against AA. While LPTGWLM, MFE and GPAHCLL as most active inhibitor of AG and HLPGRG, QNVLPLH and PLMLP were predicted to be active against DPP-IV. Overall, BC and CC hydrolysates can be proposed to be used in different food formulations as functional antidiabetic agents.

AB - Camel milk proteins are an important substrate for bioactive peptides generation. This study investigates in-vitro antidiabetic effect (via inhibition of α-amylase (AA), α-glucosidase (AG) and dipeptidyl peptidase IV (DPP-IV)) of bovine (BC) and camel casein (CC) hydrolysates. Further, effect of simulated gastrointestinal digestion (SGID) on inhibitory potential of generated hydrolysates was also explored. Both BC and CC hydrolysates displayed potent inhibitory properties against AA (IC50 value- 0.58 & 0.59 mg/mL), AG (IC50 value- 1.04 & 0.59 mg/mL) and DPP-IV (IC50 value- 0.62 & 0.66 mg/mL), respectively. Among different peptides identified in BC and CC hydrolysates, it was observed that FLWPEYGAL was predicted to be most potent inhibitory peptide against AA. While LPTGWLM, MFE and GPAHCLL as most active inhibitor of AG and HLPGRG, QNVLPLH and PLMLP were predicted to be active against DPP-IV. Overall, BC and CC hydrolysates can be proposed to be used in different food formulations as functional antidiabetic agents.

KW - Anti-diabetic

KW - Bovine casein

KW - Camel casein

KW - Dipeptidyl peptidase-IV (DPP-IV)

KW - Peptide sequencing

KW - Protein hydrolysates

KW - α-Amylase (AA)

KW - α-Glucosidase (AG)

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U2 - 10.1016/j.foodchem.2021.129374

DO - 10.1016/j.foodchem.2021.129374

M3 - Article

C2 - 33740505

AN - SCOPUS:85102806164

SN - 0308-8146

VL - 353

JO - Food Chemistry

JF - Food Chemistry

M1 - 129374

ER -

Simulated gastrointestinal digestion of camel and bovine casein hydrolysates: Identification and characterization of novel anti-diabetic bioactive peptides

Abstract

Keywords

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