Calcium-binding peptides derived from tilapia (Oreochromis niloticus) protein hydrolysate

Charoenphun, Narin; Cheirsilp, Benjamas; Sirinupong, Nualpun; Youravong, Wirote

doi:10.1007/s00217-012-1860-2

Cited by 90 publications

(58 citation statements)

References 27 publications

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“…The ortho-phthalaldehyde (OPA) method described by Charoenphun et al [25] was used to estimate DH with some modifications. The freshly prepared reagent consisted of 6 mM OPA (dissolved in methanol) and 0.2% (v/v) 2-mercaptoethanol in 50 mM sodium tetraborate containing 1% (w/v) SDS.…”

Section: Methodsmentioning

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.

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Section: Methodsmentioning

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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“…The measurement of Ca chelating activity was carried out by the method described in previous studies (Charoenphun, Cheirsilp, Sirinupong, & Youravong, 2013;Jung & Kim, 2007). Peptide sample (0.5 mg/ml) was mixed with 5 mmol/l CaCl 2 in 20 mmol/l sodium phosphate buffer (pH 7.5) and incubated at 37°C for 30 min.…”

Section: Ca Chelating Activitymentioning

confidence: 99%

Fractionation and identification of Alaska pollock skin collagen-derived mineral chelating peptides

et al. 2015

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“…Considering nutritional quality and cost, many animal sources, aquatic sources and plant sources are suitable as protein sources to produce protein hydrolysates for calcium-chelating peptides . Calciumchelating peptides have been isolated and characterised from various sources, including cow milk casein (Meisel & Frister, 1988), whey (Huang et al, 2015), tilapia fish muscle and scales (Charoenphun et al, 2013;Chen et al, 2014) and soy (Lv et al, 2013) proteins. Many studies show that the calcium-chelating activity of protein hydrolysates depends on enzymes types, degree of hydrolysis, amino acid composition, specific groups of amino acids and molecular weight Guo et al, 2014;Sun et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Optimised condition for preparing sea cucumber ovum hydrolysate–calcium complex and its structural analysis

Cui

Sun

Jiang

et al. 2017

Int J of Food Sci Tech

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Summary This study aimed to determine optimum preparation conditions of sea cucumber ovum hydrolysates–calcium (SCOHs–Ca) complexes by Box–Behnken design and further elucidate their microstructure characteristics using Fourier transform infrared spectroscopy, scanning electron microscope, atomic force microscopy and dynamic light scattering. The predicted calcium‐chelating capacity under the optimum conditions of the process variables was very close to the experimental value (53.45 ± 0.29 mg g−1) determined in the batch experiment. Results demonstrated that the calcium bind to the SCOHs to form the SCOHs–Ca complexes primarily via interactions with carboxyl oxygen and amino nitrogen atoms. The prepared SCOHs–Ca complexes formed compact nanoparticles and exhibited a fold and porous network structure. These changes could be attributed to the interaction between peptides and calcium ions. Our findings provide a theoretical basis for the development of new calcium preparations as well as the high‐value utilisation of sea cucumber by‐products.

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Calcium-binding peptides derived from tilapia (Oreochromis niloticus) protein hydrolysate

Cited by 90 publications

References 27 publications

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

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

Fractionation and identification of Alaska pollock skin collagen-derived mineral chelating peptides

Optimised condition for preparing sea cucumber ovum hydrolysate–calcium complex and its structural analysis

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