Purification, identification and molecular mechanism of two dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from Antarctic krill (Euphausia superba) protein hydrolysate

Ji, Wei; Zhang, Chaohua; Ji, Hongwu

doi:10.1016/j.jchromb.2017.09.001

Cited by 51 publications

(32 citation statements)

References 35 publications

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“…Finally, molecular docking analysis was performed to investigate the interaction mechanism between DPP-IV and DPP-IV inhibitors. Molecular docking analysis has been widely used to investigate molecular mechanism of DPP-IV inhibitory peptides [34,35]. The active site of DPP-IV contains two pockets as follows: a hydrophobic S1 pocket consisted of residues Tyr631, Val656, Trp659, Tyr662, Tyr666, and Val711; and a charged S2 pocket consisted of residues Arg125, Glu205, Glu206, Phe357, Ser209, and Arg358 [36].…”

Section: Discussionmentioning

confidence: 99%

“…As listed in Table 1, the peptide sequences of the F3-8 and F3-11 were Glu-Leu-Lys-Asp-Leu-Lys-Gly-Tyr (ELKDLKGY) and Ile-Leu-Asp-Lys-Val-Gly-Ile-Asn-Tyr (ILDKVGINY), respectively. Figure 4A showed the LC-MS/MS spectrum of single-charged ion with m/z 483.26996, which matched to sequence ELKDLKGY corresponding to bovine α-lactalbumin f (30)(31)(32)(33)(34)(35)(36)(37). Figure 4B showed the LC-MS/MS spectrum of single-charged ion with m/z 517.79901, which matched to sequence ILDKVGINY corresponding to bovine α-lactalbumin f (114-122).…”

Section: Identification Of Dpp-iv Inhibitory Peptidesmentioning

confidence: 94%

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Dipeptidyl Peptidase-IV Inhibitory Activity and Related Molecular Mechanism of Bovine α-Lactalbumin-Derived Peptides

2020

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Identifying DPP-IV inhibitory peptides from dietary protein has attracted increased attention. In the present study, bovine α-lactalbumin hydrolysates were generated by alcalase for various hydrolysis times, and DPP-IV inhibitory activity of these hydrolysates was determined. The 4 h hydrolysates displayed the most potent DPP-IV inhibitory activity, with DPP-IV inhibition rate of 82.30 ± 1.39% at concentration of 1.0 mg/mL. DPP-IV inhibitory peptides were isolated from the 4 h-hydrolysates with gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). Using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI MS/MS), two DPP-IV inhibitory peptides were identified, and their amino acid sequences were Glu-Leu-Lys-Asp-Leu-Lys-Gly-Tyr (ELKDLKGY) and Ile-Leu-Asp-Lys-Val-Gly-Ile-Asn-Tyr (ILDKVGINY), respectively. Furthermore, molecular docking analysis showed that peptides ELKDLKGY and ILDKVGINY could form hydrogen bonds, pi-cation interactions, and salt bridges with DPP-IV. These findings indicated that bovine α-lactalbumin may be a potential source of natural DPP-IV inhibitor.

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Section: Discussionmentioning

confidence: 99%

Section: Identification Of Dpp-iv Inhibitory Peptidesmentioning

confidence: 94%

Dipeptidyl Peptidase-IV Inhibitory Activity and Related Molecular Mechanism of Bovine α-Lactalbumin-Derived Peptides

2020

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“…Combination of two or three of the above chromatography methods should achieve peptide purification. Song et al, Huang et al, and Ji et al combined gel filtration chromatography and C 18 chromatography to purify DPP-IV inhibitory peptides [37,38,39]. Harnedy et al used a C 18 matrix solid-phase extraction (SPE) column followed by Semipreparative reversed-phase high performance liquid chromatography (SP RP-HPLC) to obtain three purified DPP-IV inhibitory peptides [40].…”

Section: Methods For Discovering Food-derived Dpp-iv Inhibitory Pementioning

confidence: 99%

Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review

Liu

Cheng

2019

IJMS

119

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Diabetes is a chronic metabolic disorder which leads to high blood sugar levels over a prolonged period. Type 2 diabetes mellitus (T2DM) is the most common form of diabetes and results from the body’s ineffective use of insulin. Over ten dipeptidyl peptidase IV (DPP-IV) inhibitory drugs have been developed and marketed around the world in the past decade. However, owing to the reported adverse effects of the synthetic DPP-IV inhibitors, attempts have been made to find DPP-IV inhibitors from natural sources. Food-derived components, such as protein hydrolysates (peptides), have been suggested as potential DPP-IV inhibitors which can help manage blood glucose levels. This review focuses on the methods of discovery of food-derived DPP-IV inhibitory peptides, including fractionation and purification approaches, in silico analysis methods, in vivo studies, and the bioavailability of these food-derived peptides. Moreover, food-derived DPP-IV inhibitory peptides discovered during this decade are listed and distributed in a 3D scatter plot graph based on their IC50, molecular weight, and grand average of hydropathicity values, which can help us to understand the relationship between the features of the peptides and their activities.

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“…Unused fish parts may have greater nutritional value than the main product (FAO, ; Kim & Mendis, ). Although available in abundance, krill, a high‐protein source, remains underutilized due to its small size (Ji, Zhang, & Ji, ). Of the estimated 1000 billion MT available, a small percentage is caught (0.006–0.01%) (Ji et al, ; Putland & Sutton, ), and less of that is used for human consumption (Ichii, ; Matak, Tahergorabi, & Jaczynski, ).…”

Section: Nontraditional Protein Sourcesmentioning

confidence: 99%

“…Although available in abundance, krill, a high‐protein source, remains underutilized due to its small size (Ji, Zhang, & Ji, ). Of the estimated 1000 billion MT available, a small percentage is caught (0.006–0.01%) (Ji et al, ; Putland & Sutton, ), and less of that is used for human consumption (Ichii, ; Matak, Tahergorabi, & Jaczynski, ). Krill protein content ranges from 11.9% to 15.4% (crude) or 60% to 65% (dwb) and contains all essential amino acids (Food and Agriculture Organization/World Health Organization/United Nations University, ).…”

Section: Nontraditional Protein Sourcesmentioning

confidence: 99%

Protein Solubilization

Sathe

Zaffran

Gupta

et al. 2018

J Americ Oil Chem Soc

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To address the anticipated global need for increased protein supply for human nutrition, particularly for developing and underdeveloped regions, concerted efforts are required. Although animal proteins satisfy nutrition needs, they may not be acceptable to all consumers either due to their cost or dietary restrictions followed by the consumer. Soybean has served as a nonanimal protein source; however, alternative protein sources will need to be cultivated and explored in the future to satisfy anticipated increased global needs. To effectively utilize a food protein source, separation of proteins from the nonprotein components present in that source is often needed or desired. Such separation requires understanding of protein properties and interactions of the protein with its environment. In chemical separation processes, protein solubility is a critical property as it often governs protein preparation and utilization and is the focus of this review. Emphasis is on nontraditional protein sources. J Am Oil Chem Soc (2018) 95: 883-901 884 J Am Oil Chem Soc J Am Oil Chem Soc (2018) 95: 883-901 1:100 c 2-98 Thompson, 1977 885 J Am Oil Chem Soc J Am Oil Chem Soc (2018) 95: 883-901 J Am Oil Chem Soc J Am Oil Chem Soc (2018) 95: 883-901

show abstract

Purification, identification and molecular mechanism of two dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from Antarctic krill (Euphausia superba) protein hydrolysate

Cited by 51 publications

References 35 publications

Dipeptidyl Peptidase-IV Inhibitory Activity and Related Molecular Mechanism of Bovine α-Lactalbumin-Derived Peptides

Dipeptidyl Peptidase-IV Inhibitory Activity and Related Molecular Mechanism of Bovine α-Lactalbumin-Derived Peptides

Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review

Protein Solubilization

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