Whey as a source of peptides with remarkable biological activities

http://digital.csic.es/bitstream/10261/171169/4/releasegastrodigest.pdf

Release of dipeptidyl peptidase IV, α-amylase and α-glucosidase inhibitory peptides from quinoa (Chenopodium quinoa Willd.) during in vitro simulated gastrointestinal digestion

Type 2 diabetes (T2D), one of the major common human health problems, is growing at an alarming rate around the globe. Alpha-glucosidase and dipeptidyl peptidase IV (DPP-IV) enzymes play a significant role in development of T2D. Hence, reduction or inhibition of their activity can be one of the important strategies in management of T2D. Studies in the field of bioactive peptides have shown that dietary proteins could be natural source of alpha-glucosidase and DPP-IV inhibitory peptides. The purpose of this review is to provide an overview of food protein-derived peptides as potential inhibitors of alpha-glucosidase and DPP-IV with major focus on milk proteins. Efforts have been made to review the available information in literature on the relationship between food protein-derived peptides and T2D. This review summarizes the current data on alpha-glucosidase and dipeptidyl peptidase IV inhibitory bioactive peptides derived from proteins and examines the potential value of these peptides in the treatment and prevention of T2D. In addition, the proposed modes of inhibition of peptide inhibitors are also discussed. Studies revealed that milk and other food proteins-derived bioactive peptides play a vital role in controlling T2D through several mechanisms, such as the satiety response, regulation of incretin hormones, insulinemia levels, and reducing the activity of carbohydrate degrading digestive enzymes. The bioactive peptides could be used in prevention and management of T2D through functional foods or nutraceutical supplements. Further clinical trials are necessary to validate the findings of in vitro studies and to confirm the efficiency of these peptides for applications.

Food protein-derived bioactive peptides in management of type 2 diabetes

Background Diabetes, which currently affects 1 in 11 adults, is considered one of the biggest worldwide health crises of the 21st century. Over the last decade, synthetic inhibitors of the enzyme dipeptidyl-peptidase IV (DPP-IV) have emerged as an effective pharmaceutical approach for the management of type 2 diabetes. These molecules exert their beneficial effect by preventing the inactivation of gut-derived hormones that play a pivotal role in glycemic regulation. More recently, food components have been suggested as sources of DPP-IV inhibitors with the potential to help manage blood glucose levels. Scope and approach This review examines the sources, production, molecular characteristics and modes of action of food-derived DPP-IV inhibitors. Insights into the needs for future research to validate their efficacy and to establish their application in the management of type 2 diabetes are also discussed. Key findings and conclusions To date, hydrolysates of protein from a variety of food commodities, including both plant and animal sources, have been shown to be able to inhibit the activity of the DPP-IV enzyme. Moreover, a number of peptides, either isolated from these hydrolysates or synthetically produced, as well as non-protein-derived compounds such as polyphenols, have also been identified as DPP-IV inhibitors. These food-derived constituents present different degrees of potency and modes of action on the DPP-IV enzyme. While their effectiveness in humans is currently unknown, findings from in vitro and animal studies conducted to date warrant further research to evaluate their potential as functional food ingredients for glycemic regulation.

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Food-derived dipeptidyl-peptidase IV inhibitors as a potential approach for glycemic regulation : current knowledge and future research considerations

Proteins are a potential source of health-promoting biomolecules with medical, nutraceutical, and food applications. Nowadays, bioactive peptides production, its isolation, characterization, and strategies for its delivery to target sites are a matter of intensive research. In vitro and in vivo studies regarding the bioactivity of peptides has generated strong evidence of their health benefits. Dairy proteins are considered the richest source of bioactive peptides, however proteins from animal and vegetable origin also have been shown to be important sources. Enzymatic hydrolysis has been the process most commonly used for bioactive peptide production. Most commercial enzymatic preparations frequently used are from animal (e.g., trypsin and pepsin) and microbial (e.g., Alcalase® and Neutrase®) sources. Although the use of plant proteases is still relatively limited to papain and bromelain from papaya and pineapple, respectively, the application of new plant proteases is increasing. This review presents the latest knowledge in the use and diversity of plant proteases for bioactive peptides release from food proteins including both available commercial plant proteases as well as new potential plant sources. Furthermore, the properties of peptides released by plant proteases and health benefits associated in the control of disorders such as hypertension, diabetes, obesity, and cancer are reviewed.

Plant proteases for bioactive peptides release: A review

In the present study, whey protein concentrate (WPC-80) and β-lactoglobulin were hydrolyzed with a noncommercial serine protease isolated from Asian pumpkin (Cucurbita ficifolia) Hydrolysates were further fractionated by ultrafiltration using membranes with cut-offs equal 3 and 10 kDa Peptide fractions of molecular weight lower than 3 and 3–10 kDa were further subjected to the RP-HPLC Separated preparations were investigated for their potential as the natural inhibitors of dipeptidyl peptidase (DPP-IV), α-glucosidase and angiotensin converting enzyme (ACE) WPC-80 hydrolysate showed higher inhibitory activities against the three tested enzymes than β-lactoglobulin hydrolysate Especially high biological activities were exhibited by peptide fractions of molecular weight lower than 3 kDa, with ACE IC50 <064 mg/mL and DPP-IV IC50 <055 mg/mL This study suggests that peptides generated from whey proteins may support postprandial glycemia regulation and blood pressure maintenance, and could be used as functional food ingredients in the diet of patients with type 2 diabetes

/pdf/the-evaluation-of-dipeptidyl-peptidase-dpp-iv-a-glucosidase-3mkysx8abg.pdf

The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia)

Dąbrowska Anna

Papers

The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia)