Functional yogurt fortified with fish collagen‐derived bioactive peptides: Antioxidant capacity, ACE and DPP‐IV inhibitory

Author(s):  
Samaneh Ayati ◽  
Jong‐Bang Eun ◽  
Najme Atoub ◽  
Armin Mirzapour‐Kouhdasht

2021 ◽  
Vol 22 (17) ◽  
pp. 9508
Author(s):  
Nhung Thi Phuong Nong ◽  
Jue-Liang Hsu

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.



2021 ◽  
Vol 104 (1) ◽  
pp. 61-77
Author(s):  
Arshida Ashraf ◽  
Priti Mudgil ◽  
Abdulrasheed Palakkott ◽  
Rabah Iratni ◽  
Chee-Yuen Gan ◽  
...  


Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2910 ◽  
Author(s):  
Fenny Panjaitan ◽  
Honey Gomez ◽  
Yu-Wei Chang

Major proteins contained in dried giant grouper roe (GR) such as vitellogenin (from Epinephelus coioides; NCBI accession number: AAW29031.1), apolipoprotein A-1 precursor (from Epinephelus coioides; NCBI accession number: ACI01807.1) and apolipoprotein E (from Epinephelus bruneus; NCBI accession number: AEB31283.1) were characterized through compiled proteomics techniques (SDS-PAGE, in-gel digestion, mass spectrometry and on-line Mascot database analysis). These proteins were subjected to in silico analysis using BLAST and BIOPEP-UWM database. Sequence similarity search by BLAST revealed that the aligned vitellogenin sequences from Epinephelus coioides and Epinephelus lanceolatus share 70% identity, which indicates that the sequence sample has significant similarity with proteins in sequence databases. Moreover, prediction of potential bioactivities through BIOPEP-UWM database resulted in high numbers of peptides predominantly with dipeptidyl peptidase-IV (DPP-IV) and angiotensin-I-converting enzyme (ACE-I) inhibitory activities. Pepsin (pH > 2) was predicted to be the most promising enzyme for the production of bioactive peptides from GR protein, which theoretically released 82 DPP-IV inhibitory peptides and 47 ACE-I inhibitory peptides. Overall, this work highlighted the potentiality of giant grouper roe as raw material for the generation of pharmaceutical products. Furthermore, the application of proteomics and in silico techniques provided rapid identification of proteins and useful prediction of its potential bioactivities.



2021 ◽  
pp. 32-35
Author(s):  
Ксения Александровна Рязанцева ◽  
Евгения Юрьевна Агаркова

Целью данного исследования являлся скрининг биопептидов, высвобождаемых из белков молочной сыворотки с использованием базы данных BIOPEP. В задачи работы входили оценка сывороточных белков как потенциальных предшественников биоактивных пептидов с последующей оценкой их потенциальной биологической активности, моделирование ферментативного гидролиза и оценка полученного пептидного профиля. Объектами исследований являлись белки молочной сыворотки и ферментные препараты трипсин EC (3.4.21.4), химотрипсин EC (3.4.21.1) и алкалаза (EC 3.4.21.62). Методы исследований включали in silico анализ с использованием базы данных BIOPEP-UWM™. В результате исследований в бета-лактоглобулине была определена наибольшая частота встречаемости гипотензивных пептидов, ингибирующих ангиотензин-I-превращающий фермент (АПФ) (A=0,5528), и противодиабетических, ингибирующих дипептидилпептидазу IV (ДПП-IV) (A=0,6584), суммарная доля которых составила более 65 % среди всех потенциальных биопептидов. Наилучший результат при дальнейшем моделировании in silico гидролиза бета-лактоглобулина был получен с использованием трипсина, химотрипсина и алкалазы. Показано, что данные ферменты способствуют выделению пептидов с высокими значениями IC50: гипотензивные (VY [41-42] (IC50 = 7,1 мкМ), VF [80-81] (IC50 = 9,2 мкМ), VY [41-42] (IC50 = 7,1 мкМ), IIAEK [70-74] (IC50 = 63,7 мкМ), VR [122-123] (IC50 = 141мкМ) и противодиабетические (VL [91-92] (IC50 = 74 мкМ), IPAVF (IC50 = 44,7 мкМ), VR [122-123] (IC50 = 52,8 мкМ). Данные проведенного биоинформационного подхода определили условия для последующего воспроизведения на реальных пищевых белковых системах. The aim of this study was to screen for biopeptides released from whey proteins using the BIOPEP database. The tasks of the work included: assessment of whey proteins as potential precursors of bioactive peptides with subsequent assessment of their potential biological activity, modeling of enzymatic hydrolysis and assessment of the obtained peptide profile.The objects of the study were whey proteins and enzyme preparations trypsin EC (3.4.21.4), chymotrypsin EC (3.4.21.1) and Alcalase (EC 3.4.21.62). Research methods are included in silicoanalysis using the BIOPEP-UWM ™ database. As a result of studies on beta-lactoglobulin, the highest frequency of occurrence of antihypertensive peptides that inhibit angiotensin-I-converting enzyme (ACE) (A = 0.5528) and antidiabetic peptides that inhibit dipeptidyl peptidase IV (DPP-IV) (A = 0.6584) was obtained, the total share of which was more than 65 % among all potential biopeptides. The best result in further in silico modeling of beta-lactoglobulin hydrolysis was obtained using trypsin, chymotrypsin, and alkalase. These enzymes were shown to promote the release of peptides with high IC50 values: hypotensive (VY [41-42] (IC50 = 7.1 μM), VF [80-81] (IC50 = 9.2 μM), VY [41-42] (IC50 = 7.1 μM), IIAEK [70-74] (IC50 = 63.7 μM), VR [122-123] (IC50 = 141 μM) and antidiabetic (VL [91-92] (IC50 = 74 μM), IPAVF (IC50 = 44.7 μM), VR [122-123] (IC50 = 52.8 μM). The data of the bioinformatic approach carried out determined the conditions for subsequent reproduction on real food protein systems.



Author(s):  
Arshida Ashraf ◽  
Priti Mudgil ◽  
Abdulrasheed Palakkott ◽  
Rabah Iratni ◽  
Chee-Yuen Gan ◽  
...  


2019 ◽  
Vol 20 (20) ◽  
pp. 5191 ◽  
Author(s):  
Honey Lyn R. Gomez ◽  
Jose P. Peralta ◽  
Lhumen A. Tejano ◽  
Yu-Wei Chang

In this study, the potential bioactivities of Portuguese oyster (Crassostrea angulata) proteins were predicted through in silico analyses and confirmed by in vitro tests. C. angulata proteins were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and identified by proteomics techniques. Hydrolysis simulation by BIOPEP-UWM database revealed that pepsin (pH > 2) can theoretically release greatest amount of bioactive peptides from C. angulata proteins, predominantly angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory peptides, followed by stem bromelain and papain. Hydrolysates produced by pepsin, bromelain and papain have shown ACE and DPP-IV inhibitory activities in vitro, with pepsin hydrolysate (PEH) having the strongest activity of 78.18% and 44.34% at 2 mg/mL, respectively. Bioactivity assays of PEH fractions showed that low molecular weight (MW) fractions possessed stronger inhibitory activity than crude hydrolysate. Overall, in vitro analysis results corresponded with in silico predictions. Current findings suggest that in silico analysis is a rapid method to predict bioactive peptides in food proteins and determine suitable enzymes for hydrolysis. Moreover, C. angulata proteins can be a potential source of peptides with pharmaceutical and nutraceutical application.



Author(s):  
Erwann Durand ◽  
Sophie Beaubier ◽  
Isidora Ilic ◽  
Frederic fine ◽  
Romain Kapel ◽  
...  


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