Isolation of a calcium-binding peptide from tilapia scale protein hydrolysate and its calcium bioavailability in rats

Chen, Da; Mu, Xinmin; Huang, Hai; Nie, Ruiyan; Liu, Zunying; Zeng, Mingyong

doi:10.1016/j.jff.2013.12.001

Cited by 125 publications

(105 citation statements)

References 38 publications

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“…The mice in the normal group (ten mice) were fed normal diet throughout the feeding process. In the case of low‐Ca groups (50 mice), the feeding process was separated into two phases according to the report by Chen et al . In phase I of the 4 week feeding process, the mice were fed low‐Ca diet to establish a Ca‐deficient model.…”

Section: Methodsmentioning

confidence: 99%

“…Recent studies have revealed that excellent calcium supplements could be prepared from fish by‐products, including hoki bone, hoki frame and tilapia scales . However, those calcium‐binding peptides were isolated by hydroxyapatite affinity chromatography, gel permeation chromatography and reverse phase high‐performance liquid chromatography, and the method did not seem to be suitable for large‐scale industrial production owing to the high cost and complexity of its application.…”

Section: Introductionmentioning

confidence: 99%

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Preparation and bioavailability of calcium‐chelating peptide complex from tilapia skin hydrolysates

et al. 2017

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Preparation and bioavailability of calcium‐chelating peptide complex from tilapia skin hydrolysates

et al. 2017

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“…These preferable amino acids were not found in the peptide Leu-Arg. In addition to the amino acid composition, the spatial structure formed through mutually interaction among amino acid residues in the peptide may affect calcium affinity [26]. Further study will be required to test this possibility.…”

Section: Purification and Identification Of Peptides From Soop-camentioning

confidence: 99%

Preparation, characterization and identification of calcium-chelating Atlantic salmon (Salmo salar L.) ossein oligopeptides

Liu

Gao

et al. 2015

Eur Food Res Technol

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“…Peptides from tilapia by-products displayed various biological activities as well. A calcium-binding peptide isolated from tilapia scale protein hydrolysate was discovered to prevent calcium deficiency with improved calcium bioavailability in rats [12]. …”

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

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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

Isolation of a calcium-binding peptide from tilapia scale protein hydrolysate and its calcium bioavailability in rats

Cited by 125 publications

References 38 publications

Preparation and bioavailability of calcium‐chelating peptide complex from tilapia skin hydrolysates

Preparation and bioavailability of calcium‐chelating peptide complex from tilapia skin hydrolysates

Preparation, characterization and identification of calcium-chelating Atlantic salmon (Salmo salar L.) ossein oligopeptides

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

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