@article {8887,
	title = {Inhibition of dipeptidyl peptidase-IV by hydrolysates of beta-lactoglobulin isolated from Gir cow milk [Mass Spectrometry - Proteomics]},
	journal = {Food Chemistry Advances},
	year = {2024},
	pages = {100842},
	abstract = {<p>The current study attempts to assess the dipeptidyl peptidase {\textendash} IV (DPP-IV) inhibitory potential of β-lactoglobulin (β-Lg) isolated from milk of Gir cow. Whey was separated from skim milk by precipitation of casein followed by ultrafiltration (UF) to remove lactose and salts as permeate. β-Lg was separated from the UF retentate using salting out technique. Its purity was confirmed by SDS-PAGE and RP-HPLC. Hydrolysates of β-Lg were prepared using three different enzymes viz., pepsin, trypsin and Flavourzyme at different enzyme to substrate (E:S) ratios (1:25, 1:50, 1:100) and treated for 2-12 h durations. Pepsin-treated hydrolysate showed maximum DPP-IV inhibition of 77.62 {\textpm} 0.98 \% (IC50 =3.78 mg/mL). Hydrolysate was passed serially through UF filters of 10 and 3 kDa. The permeate of 3 kDa, which exhibited 52.10 {\textpm} 0.72 \% DPP-IV inhibition was fractionated through RP-HPLC and time based fractions were collected. All 41 fractions were again analysed for DPP-IV inhibition activity and 3 fractions which showed maximum DPP-IV inhibition activity were chosen for LC-MS/MS analysis. One novel peptide was identified through LC-MS/MS, which showed adequate DPP-IV inhibition (IC50 = 6.64 mmolL-1).</p>
},
	keywords = {Antidiabetic peptides, Degree of hydrolysis, DPP-IV inhibition, IC value, β-lactoglobulin},
	issn = {2772-753X},
	doi = {https://doi.org/10.1016/j.focha.2024.100842},
	url = {https://www.sciencedirect.com/science/article/pii/S2772753X24002375},
	author = {Ashok Kumar and M H Sathish Kumar and C S Rajani and Latha Sabikhi and Harshita Sonarthi}
}
