Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions

Fu, Yu; Young, Jette F.; Løkke, Mette Marie; Lametsch, René; Aluko, Rotimi E.; Therkildsen, Margrethe

doi:10.1016/j.jff.2016.03.026

Cited by 100 publications

(53 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In silico approach provides an alternative strategy for the investigation of novel bioactive peptides, but also has its limitations. Previous results showed that the products of enzymatic hydrolysis changed with the degree of hydrolysis, which was affected by kinds of factors, such as protein structural features, enzymatic activity, temperature, pH, hydrolysis time, and enzyme–substrate ratios (Fu et al, ; Han et al, ; Tu et al, ). However, the enzymolysis by in silico tools was rather idealistic, the digestion happened in every specific cutting site of enzymes, and it was carried out completely.…”

Section: Resultsmentioning

confidence: 99%

Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Guo

Richel

Hao

et al. 2020

Food Science & Nutrition

View full text Add to dashboard Cite

Quinoa protein has been paid more and more attention because of its nutritional properties and beneficial effects. With the development of bioinformatics, bioactive peptide database and computer‐assisted simulation provide an efficient and time‐saving method for the theoretical estimation of potential bioactivities of protein. Therefore, the potential of quinoa protein sequences for releasing bioactive peptides was evaluated using the BIOPEP database, which revealed that quinoa protein, especially globulin, is a potential source of peptides with dipeptidyl peptidase‐IV (DPP‐IV) and angiotensin‐I‐converting enzyme (ACE) inhibitory activities. Three plant proteases, namely papain, ficin, and stem bromelain, were employed for the in silico proteolysis of quinoa protein. Furthermore, four tripeptides (MAF, NMF, HPF, and MCG) were screened as novel promising bioactive peptides by PeptideRanker. The bioactivities of selected peptides were confirmed using chemical synthesis and in vitro assay. The present work suggests that quinoa protein can serve as a good source of bioactive peptides, and in silico approach can provide theoretical assistance for investigation and production of functional peptides.

show abstract

Section: Resultsmentioning

confidence: 99%

Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Guo

Richel

Hao

et al. 2020

Food Science & Nutrition

View full text Add to dashboard Cite

show abstract

“…Among the peptides identified from nebulin, the ACE inhibitory activity of HGR (IC 50 = 106 ± 0.52 µM) was higher than that of EGF (IC 50 = 474.65 ± 0.08 µM) and VDF (IC 50 = 439.27 ± 0.09 µM). Furthermore, ACE inhibitory activity of peptide HGR was stronger than that of peptide TLVGR (IC 50 = 249.3 µM) from hazelnut (Liu, Fang, Min, Liu, & Li, 2018), LY (110 µM), TF (810 µM), and RALP (650 µM) from rapeseed (He et al, 2013b), WYT (IC 50 = 574 µM) from hemp seed (Girgih, He, & Aluko, 2014), GPR (IC 50 = 132.8 µM) from bovine collagen (Fu et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

Novel Angiotensin‐Converting Enzyme Inhibitory Peptides Derived from Oncorhynchus mykiss Nebulin: Virtual Screening and In Silico Molecular Docking Study

Yang

Zhao

et al. 2018

Journal of Food Science

View full text Add to dashboard Cite

show abstract

“…Although the application of bioactive peptide database is efficient in choosing appropriate proteases, overlooking the interference factors associated with in vitro digestion could lead to discordance between in silico and in vitro methods [20]. In silico methods are used initially to assess the effectiveness of the enzyme-produced bioactive peptides.…”

Section: Introductionmentioning

confidence: 99%

Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates

Lin

Alashi

Aluko

et al. 2017

Food & Nutrition Research

Self Cite

View full text Add to dashboard Cite

Proteins from tilapia frame and skin can potentially be precursors of antihypertensive peptides according to the result of BIOPEP analyses. The aim was to generate peptides with inhibitory effects against angiotensin-converting enzyme (ACE) and renin from tilapia frame and skin protein isolates (FPI and SPI). The most active hydrolysate was then tested for blood pressure-lowering ability in spontaneously hypertensive rats (SHRs). Tilapia frame and skin protein hydrolysates (FPHs and SPHs) were respectively produced from FPI and SPI hydrolysis using pepsin, papain, or bromelain. The ACE-inhibitory activities of tilapia protein hydrolysates with varying degree of hydrolysis (DH) were evaluated. In order to enhance the activity, the hydrolysate was fractionated into four fractions (<1 kDa, 1–3 kDa, 3–5 kDa, and 5–10 kDa) and the one with the greatest ability to inhibit in vitro ACE and renin activities was subjected to oral administration (100 mg/kg body weight) to SHRs. Systolic and diastolic blood pressure (SBP and DBP), mean arterial pressure (MAP), and heart rates (HR) were subsequently measured within 24 h. The pepsin-hydrolyzed FPH (FPHPe) with the highest DH (23%) possessed the strongest ACE-inhibitory activity (IC50: 0.57 mg/mL). Its <1 kDa ultrafiltration fraction (FPHPe1) suppressed both ACE (IC50: 0.41 mg/mL) and renin activities more effectively than larger peptides. In addition, FPHPe1 significantly (p < 0.05) reduced SBP (maximum −33 mmHg), DBP (maximum −24 mmHg), MAP (maximum −28 mmHg), and HR (maximum −58 beats) in SHRs. FPHPe1 showed both in vitro and in vivo antihypertensive effects, which suggest tilapia processing coproducts may be valuable protein raw materials for producing antihypertensive peptides.

show abstract

Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions

Cited by 100 publications

References 54 publications

Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Novel Angiotensin‐Converting Enzyme Inhibitory Peptides Derived from Oncorhynchus mykiss Nebulin: Virtual Screening and In Silico Molecular Docking Study

Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates

Contact Info

Product

Resources

About