Antiproliferative activity of peptides prepared from enzymatic hydrolysates of tuna dark muscle on human breast cancer cell line MCF-7

Hsu, Kuo‐Chiang; Li‐Chan, Eunice C.Y.; Jao, Chia-Ling

doi:10.1016/j.foodchem.2010.11.066

Cited by 155 publications

(80 citation statements)

References 28 publications

(39 reference statements)

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“…Antiproliferative activity of rohu roe protein hydrolysates was determined by the MTT (3-(4,5-dimethylthiazol-2-yl) 2,5-diphenyl tetrazolium bromide) assay (Hsu et al 2011). The Caco-2 cells (human epithelial colorectal adenocarcinoma cells) were obtained from National Centre for Cell Science (NCCS), Pune, India and seeded in a 96-well flat bottom plate at a density of 1 × 10 4 cells/well in 100 μl of DMEM medium supplemented with 10 % foetal bovine serum (FBS), Lglutamine and streptomycin 125 mg/L.…”

Section: Antiproliferative Activity On Caco-2 Cell Linementioning

confidence: 99%

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Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

et al. 2015

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Previously, we have reported the chemical composition, molecular mass distribution and antioxidant activity of rohu roe protein hydrolysates. In the current study, antiproliferative, angiotensin-converting enzyme (ACE)-inhibitory activities and functional properties of protein hydrolysates from rohu (Labeo rohita) roe proteins, prepared by gastrointestinal proteases (pepsin and trypsin), were investigated. Antiproliferative activity was evaluated against human colon cancer cell line Caco-2. The results showed that the pepsin hydrolysate possessed dose dependent inhibitory effect on Caco-2 cell line. Pepsin and trypsin hydrolysates displayed ACE-inhibitory activity in vitro. The ACE-inhibitory activity of the hydrolysate generated by pepsin (47 ± 1.7 %, at 1 mg/ml) is higher than that obtained by trypsin (36 ± 3.2 %). Additionally, the undigested rohu roe proteins and its hydrolysates exhibited functional properties. Solubilities of the hydrolysates were above 81 ± 9.2 % at all pH values tested. Pepsin and trypsin hydrolysates showed good foaming capacity (45-211 %) and emulsification activity (4-29 m 2 /g). The foaming abilities and emulsifying activity index (EAI) were affected by pH. The results suggest that protein hydrolysates from rohu roe could be useful in food industry for various applications.

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Section: Antiproliferative Activity On Caco-2 Cell Linementioning

confidence: 99%

“…Picot et al (2006) reported antiproliferative activity for fish protein hydrolysates. Protein hydrolysates from tuna dark muscle, anchovy sauce, soybean, egg, milk, rice have been extensively investigated for anticancer activity (Hsu et al 2011;Lee et al 2003;Shahidi and Zhong 2008;Revilla et al 2013).…”

Section: Introductionmentioning

confidence: 99%

Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

et al. 2015

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“…GLSDGEWQ strongly inhibited the proliferation of AGS cells, while none of tested peptides had a cytotoxic effect on A549 cells (Jang et al, 2008;Ryan et al, 2011;Udenigwe and Ashton, 2013). Hsu et al (2011) isolated two peptides from tuna dark muscle which was treated with two proteases, papain and protease XXII. Amino acid sequences of these peptides were LPHVLTPEAGAT from papain hydrolysate and PTAEGVYMVT, from protease XXIII and both of them exhibited dose-dependent antiproliferative activities against human breast adenocarcinoma (MCF-7) cells, (Hsu et al, 2011;Ryan et al, 2011;Udenigwe and Aluko, 2012).…”

Section: Anticancer Propertiesmentioning

confidence: 99%

“…Hsu et al (2011) isolated two peptides from tuna dark muscle which was treated with two proteases, papain and protease XXII. Amino acid sequences of these peptides were LPHVLTPEAGAT from papain hydrolysate and PTAEGVYMVT, from protease XXIII and both of them exhibited dose-dependent antiproliferative activities against human breast adenocarcinoma (MCF-7) cells, (Hsu et al, 2011;Ryan et al, 2011;Udenigwe and Aluko, 2012). Picot et al (2006) reported 18 protein hydrolysates isolated from blue whiting, cod, plaice, and salmon to have antiproliferative activity against 2 human breast cancer cell lines (MCF-7/6 and MDA-MB-231) (Picot et al, 2006;Shahidi and Zhong, 2008;Ryan et al, 2011).…”

Section: Anticancer Propertiesmentioning

confidence: 99%

Bioactive peptides from meat and their influence on human health

Baltić¹,

Bošković²,

Ivanović³

et al. 2014

Tehnologija mesa

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“…FPH has been made from fish by-products as well as underutilized fish species through the process of hydrolysis [4]. In [5] conducted studies of the enzymatic production of hydrolysate from tuna dark muscle, and in [6] highlighted the potential use of tuna dark muscle FPH in the pharmaceutical industry due to its antiproliferative and antioxidative effects. However, optimization of the enzymatic hydrolysis process for this fish by-product, especially that using Protamex®, has not been reported previously.…”

Section: Introductionmentioning

confidence: 99%

Optimization of enzymatic hydrolysis of skipjack tuna by-product using protamex ®: a response surface approach

Herpandi¹,

Ahmad²,

Nadiah³

et al. 2018

J. Fundam and Appl Sci.

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The goal of this study was to optimize enzymatic hydrolysis of the dark flesh of skipjack tuna (Katsuwonus pelamis). Protamex® was concentrations (1%, 1.5%, 2%, 2.5% 40 to 60 o C and times of 2 to 6 h. The experiment was performed following a five second-order central composite design w coefficients of determination for degree of hydrolysis (R2 = 0.9674) and free tryptophan content (R2 = 0.9426) indicate the suitability of the design for predicting the responses. The optimum hydrolytic conditions predicted by the response surface methodology were 3% Protamex® at pH 6.57 and 58 °C for 4 h. These conditions resulted in an experimental degree The goal of this study was to optimize enzymatic hydrolysis of the dark flesh of skipjack tuna (Katsuwonus pelamis). Protamex® was used as the hydrolytic enzyme at various centrations (1%, 1.5%, 2%, 2.5% and 3% w/w) at pHs from 6.5 to 8. Protamex® at pH 6.57 and 58 °C for 4 h. These conditions resulted in an experimental degree free tryptophan.

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Antiproliferative activity of peptides prepared from enzymatic hydrolysates of tuna dark muscle on human breast cancer cell line MCF-7

Cited by 155 publications

References 28 publications

Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

Bioactive peptides from meat and their influence on human health

Optimization of enzymatic hydrolysis of skipjack tuna by-product using protamex ®: a response surface approach

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