Production and identification of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from discarded Sardine pilchardus protein

Rivero‐Pino, Fernando; Espejo-Carpio, F. Javier; Guadix, Emilia M.

doi:10.1016/j.foodchem.2020.127096

Cited by 74 publications

(42 citation statements)

References 37 publications

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“…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%

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%

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

Nong

Hsu

2021

IJMS

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“…Hsu et al [ 51 ] reported that skin porcine gelatin hydrolyzed with alcalase reaches an IC50 of 0.06 mg/mL; Lafarga and Hayes [ 52 ] reported a bovine lung hydrolyzed with high pressure + alcalase showing an IC50 of 1.43 mg/mL. More recently, two studies [ 53 , 54 ] reported treatments with SGID after enzymatic pretreatments, showing IC50 of 4 mg/mL from sardine muscle and 0.23 mg/mL from boarfish. The hydrolysates of the present work presented an IC50 lower than those reported in literature, only comparable with those obtained by Hsu et al [ 51 ].…”

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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“…The literature reporting fish peptides with antidiabetic activity has been recently stated [59,[81][82][83]. In this context, the use of fishing discards as protein sources for value-added products is important [55,59,83,84]. The scientific community considers enzymatic hydrolysis as a helpful option for revaluing these low-quality products and increasing their potential, as they have no side effects on the patient's health.…”

Section: Protein Sourcementioning

confidence: 99%

“…Usually, the combination of both techniques is adequate to obtain fractions that can be injected into a mass spectrometer (MS) so as to identify the peptides contained therein. For example, Rivero-Pino et al [84] reported a higher DPP-IV inhibition for sardine peptides ranging from 400 to 1400 Da after fractionation with a Superdex Peptide 10/300 GL column, using a fast protein liquid chromatography system.…”

Section: Fractionationmentioning

confidence: 99%

Antidiabetic Food-Derived Peptides for Functional Feeding: Production, Functionality and In Vivo Evidences

Rivero‐Pino

Espejo-Carpio

Guadix

2020

Foods

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Bioactive peptides released from the enzymatic hydrolysis of food proteins are currently a trending topic in the scientific community. Their potential as antidiabetic agents, by regulating the glycemic index, and thus to be employed in food formulation, is one of the most important functions of these peptides. In this review, we aimed to summarize the whole process that must be considered when talking about including these molecules as a bioactive ingredient. In this regard, at first, the production, purification and identification of bioactive peptides is summed up. The detailed metabolic pathways described included carbohydrate hydrolases (glucosidase and amylase) and dipeptidyl-peptidase IV inhibition, due to their importance in the food-derived peptides research field. Then, their characterization, concerning bioavailability in vitro and in situ, stability and functionality in food matrices, and ultimately, the in vivo evidence (from invertebrate animals to humans), was described. The future applicability that these molecules have due to their biological potential as functional ingredients makes them an important field of research, which could help the world population avoid suffering from several diseases, such as diabetes.

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Production and identification of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from discarded Sardine pilchardus protein

Cited by 74 publications

References 37 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

Antidiabetic Food-Derived Peptides for Functional Feeding: Production, Functionality and In Vivo Evidences

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