Generation and characterization of dipeptidyl peptidase-IV inhibitory peptides from trypsin-hydrolyzed α-lactalbumin-rich whey proteins

Jia, Cheng-li; Hussain, Naveed; Ujiroghene, Obaroakpo Joy; Pang, Xiaoyang; Zhang, Shuwen; Lu, Jianwei; Liu, Lu; Lv, Jing

doi:10.1016/j.foodchem.2020.126333

Cited by 53 publications

(29 citation statements)

References 34 publications

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“…The dietary proteins with highly diverse sequences used as precursors to generate protein hydrolysates and peptides with DPP-IV inhibitory activities have drastically increased over the years. To date, various food commodities such as milk [4,8,35,49,79], fish [36,54], egg [1], or special ones such as quinoa [53], rapeseed [80], and tropical banded cricket [9] are well-known as DPP-IV inhibitor sources. The IC 50 values of various DPP-IV inhibitory hydrolysates collected from the data of scientific reports in the last five years (2016-2020) are summarized in Figure 4 (see original data in Table A2).…”

Section: Enzymatic Hydrolysates Of Food Proteinsmentioning

confidence: 99%

“…The performance of enzymatic hydrolysis to produce bioactive peptides will be discussed in this section. Generation of DPP-IV inhibitory peptides from food proteins can be achieved using a single protease or multiple enzymes obtained from plants (e.g., papain) [49,79,89,90], animals (e.g., pepsin, trypsin, and Corolase PP) [2,3,35,81], or microorganisms (e.g., alcalase, protamex, and flavourzyme) [9,[91][92][93]. Each protease requires the provision of specific conditions (e.g., pH and temperature, enzyme/substrate ratio, and hydrolysis time) to optimize hydrolysis efficiency or the DPP-IV inhibitory effect of hydrolysate.…”

Section: Enzymatic Hydrolysates Of Food Proteinsmentioning

confidence: 99%

“…Currently, food-derived antidiabetic peptides with lesser side effects than commercial drugs have been isolated from various dietary proteins [15,16,20]. Different food-protein hydrolysates from milk, meat products, plants, and marine organisms are high recommendations as excellent sources of bioactive peptides [2,3,[30][31][32][33][34][35][36][37][38].…”

Section: Introductionmentioning

confidence: 99%

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Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Nong

Hsu

2021

IJMS

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Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides’ efficiencies before commercial applications.

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Section: Enzymatic Hydrolysates Of Food Proteinsmentioning

confidence: 99%

Section: Enzymatic Hydrolysates Of Food Proteinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Nong

Hsu

2021

IJMS

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“…Peptides with DPPIV inhibitory activity have not received much attention, however, some interesting studies are found in the literature; Jia et al [ 50 ] prepared trypsin hydrolysates from α-lactalbumin varying parameters and subsequently subjecting to SGID, they reported IC50 values in the range of 0.41 to 0.61 mg/mL, for samples most extensively hydrolyzed. DPPIV inhibitory activity has been assessed in other hydrolyzed proteins.…”

Section: Discussionmentioning

confidence: 99%

Engineering Concanavalin B to Release Bioactive Peptides against Metabolic Syndrome

Maldonado-Torres

Jara-Romero

Rosas-Cárdenas

et al. 2021

Foods

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Metabolic syndrome is a severe public health issue characterized by multiple metabolic disturbances. Current treatments prescribe a particular drug for each of them, producing multiple side effects. As a first step towards a more integral approach, we applied our recently described methodology to design single proteins, based in the Concanavalin B scaffold (1CNV), that contain several bioactive peptides (BPs), including antioxidant and lipid-lowering activities as well as inhibitors of dipeptidyl peptidase IV (DPPIV) and the angiotensin converting enzyme. Modified Concanavalin (CNV44), the designed protein that showed the best in silico properties, was expressed in high yields in E. coli and purified to homogeneity. After in vitro digestion with gastrointestinal enzymes, all the biological activities tested where higher in CNV44 when compared to the non-modified protein 1CNV, or to other previous reports. The results presented here represent the first in vitro evidence of a modified protein with the potential to treat metabolic syndrome and open the venue for the design of proteins to treat other non-communicable diseases.

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“…Preparative high-performance liquid chromatography (prep-HPLC) is a valuable method for isolating individual constituents from complex systems including biological samples and natural products [14][15][16][17]. This method is extensively employed in numerous areas because of its excellent column efficiency, superior separation reproducibility, online detection, and automatic control [18][19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Preparative isolation of arylbutanoid‐type phenol [(‐)‐rhododendrin] with peak tailing on conventional C18 column using middle chromatogram isolated gel column coupled with reversed‐phase liquid chromatography

Dang

Wang

et al. 2020

J of Separation Science

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Reversed‐phase liquid chromatography coupled with middle chromatogram isolated gel column was employed for the efficient preparative separation of the arylbutanoid‐type phenol [(‐)‐rhododendrin] from Saxifraga tangutica. Universal C18 (XTerra C18) and XCharge C18 columns were compared for (‐)‐rhododendrin fraction analysis and preparation. Although tailing and overloading occurred on the XTerra C18 column, the positively charged reversed‐phase C18 column (XCharge C18) overcame these drawbacks, allowing for favorable separation resolution, even when loading at a on a preparative scale (3.69 mg per injection). The general separation process was as follows. First, 365.0 mg of crude (‐)‐rhododendrin was enriched from 165 g Saxifraga tangutica extract via a middle chromatogram isolated gel column. Second, separation was performed on an XTerra C18 preparative column, from which 73.8 mg of the target fraction was easily obtained. Finally, the 24.0 mg tailing peak of (‐)‐rhododendrin on XTerra C18 column was selectively purified on the XCharge C18 analytical column. These results demonstrate that the tailing nonalkaloid peaks can be effectively used for preparative isolation on XCharge C18 columns.

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Generation and characterization of dipeptidyl peptidase-IV inhibitory peptides from trypsin-hydrolyzed α-lactalbumin-rich whey proteins

Cited by 53 publications

References 34 publications

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Engineering Concanavalin B to Release Bioactive Peptides against Metabolic Syndrome

Preparative isolation of arylbutanoid‐type phenol [(‐)‐rhododendrin] with peak tailing on conventional C18 column using middle chromatogram isolated gel column coupled with reversed‐phase liquid chromatography

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