scholarly journals Characterization of Protein Hydrolysates from Fish Discards and By-Products from the North-West Spain Fishing Fleet as Potential Sources of Bioactive Peptides

Marine Drugs ◽  
2021 ◽  
Vol 19 (6) ◽  
pp. 338
Author(s):  
Andreia Henriques ◽  
José A. Vázquez ◽  
Jesus Valcarcel ◽  
Rogério Mendes ◽  
Narcisa M. Bandarra ◽  
...  

Fish discards and by-products can be transformed into high value-added products such as fish protein hydrolysates (FPH) containing bioactive peptides. Protein hydrolysates were prepared from different parts (whole fish, skin and head) of several discarded species of the North-West Spain fishing fleet using Alcalase. All hydrolysates had moisture and ash contents lower than 10% and 15%, respectively. The fat content of FPH varied between 1.5% and 9.4% and had high protein content (69.8–76.6%). The amino acids profiles of FPH are quite similar and the most abundant amino acids were glutamic and aspartic acids. All FPH exhibited antioxidant activity and those obtained from Atlantic horse mackerel heads presented the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, reducing power and Cu2+ chelating activity. On the other hand, hydrolysates from gurnard heads showed the highest ABTS radical scavenging activity and Fe2+ chelating activity. In what concerns the α-amylase inhibitory activity, the IC50 values recorded for FPH ranged between 5.70 and 84.37 mg/mL for blue whiting heads and whole Atlantic horse mackerel, respectively. α-Glucosidase inhibitory activity of FPH was relatively low but all FPH had high Angiotensin Converting Enzyme (ACE) inhibitory activity. Considering the biological activities, these FPH are potential natural additives for functional foods or nutraceuticals.

2004 ◽  
Vol 68 (12) ◽  
pp. 2477-2483 ◽  
Author(s):  
Makoto YOSHIMOTO ◽  
Rie KURATA-AZUMA ◽  
Makoto FUJII ◽  
De-Xing HOU ◽  
Kohji IKEDA ◽  
...  

2020 ◽  
Vol 10 (7) ◽  
pp. 2290 ◽  
Author(s):  
Paula Borrajo ◽  
Mirian Pateiro ◽  
Mohammed Gagaoua ◽  
Daniel Franco ◽  
Wangang Zhang ◽  
...  

In order to make the by-products generated from the porcine industry more valuable, pig livers were used in this trial to obtain protein hydrolysates. Three proteases (alcalase, bromelain, and papain) were utilized for enzymatic hydrolysis with two different durations, 4 and 8 hours. Ultrafiltration process was used for the recovery of the extracts, employing three different membrane pore sizes (30, 10, and 5 kDa). The porcine livers contained considerable amounts of protein (19.0%), considering they are almost composed of water (74.1%). The antioxidant activity of the obtained hydrolysates was investigated using four antioxidant methods (2,2-Diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, 2-2′-Azino-di-[3-ethylbenzthiazoline sulfonate] (ABTS) radical scavenging activity, ferric reducing antioxidant power assay (FRAP), and oxygen radical absorbance capacity assay (ORAC)). Antibacterial properties were also measured against Gram-negative and Gram-positive bacteria. Results indicated that the three studied factors (type of enzyme, membrane pore size, and time) significantly affected the parameters evaluated. Hydrolysates obtained at 8 hours with alcalase had the best antioxidant properties. The 30 kDa alcalase extracts exhibited the highest DPPH (562 µg Trolox/g), FRAP (82.9 µmol Fe2+/100 g), and ORAC (53.2 mg Trolox/g) activities, while for ABTS the 10 kDa alcalase showed the higher values (1068 mg ascorbic acid/100 g). Concerning the antibacterial activity, 30 kDa hydrolysates obtained with bromelain for 4 hours exhibited the highest antimicrobial capacity, providing an inhibition of 91.7%.


2011 ◽  
Vol 361-363 ◽  
pp. 748-752 ◽  
Author(s):  
Jiao Jiao Mu ◽  
Qian Cheng Zhao ◽  
Jian Wei Li

The Mercenaria mercenaria protein hydrolysates (MMPH) and Ruditapes philippinarum protein hydrolysates (RPPH) were prepared by three enzymatic methods, and the radical scavenging activity of the protein hydrolysates was analyzed. The results showed that the protein hydrolysates prepared by the combination of Protamex and Flavourzyme exhibited significant radical scavenging activity; For DPPH radical, the EC50values of MMPH and RPPH were 33.0 mg/mL and 93.0 mg/mL, respectively, and for hydroxyl radical, the EC50values of the protein hydrolysates were 7.5 mg/mL and 7.0 mg/mL, respectively; The protein hydrolysates were further fractionated by ultrafiltration membrane of 6000 Da, and the radical scavenging activity of the resultant fraction with lower molecular weight (<6000 Da) was significantly (P<0.05) increased, and for DPPH radical, the EC50values of MMPH and RPPH fractions were 29.5 mg/mL and 58.5 mg/mL, respectively, and for hydroxyl radical, the EC50 values of the fractions were 6.0 mg/mL and 7.0 mg/mL, respectively.


2021 ◽  
Vol 12 (2) ◽  
pp. 1-7
Author(s):  
Wan Amalina Wan Mamat ◽  
Syed Ahmad Tajudin Tuan Johari ◽  
Muhammad Yusran Abdul Aziz ◽  
Ahmad Syibli Othman ◽  
Abdul Manaf Ali

Catunaregam tomentosa (Blume ex DC) Tirveng is commonly known as Khet in Thailand and Bisa Ular or Badang in Malaysia. The tree is widely distributed in the north-east region of Thailand while in Malaysia the tree usually grows in the open waterfront area at Terengganu. This plant belongs to the Rubiaceae family, and the genus catunaregam has interesting pharmacological activities such as anti-inflammatory, antispasmodic, antidysenteric, antifertility and immunomodulatory. In this study, the leaves were extracted using dichloromethane, ethyl acetate and ethanol. Total phenolic was determined by Folin-Ciocalteau method while total flavonoid was determined by the aluminium chloride calorimetric method. Meanwhile, its antioxidant activity was evaluated by the 2,2-diphenyl-1-picrylhydrazyl (DPPH) assay. The ethanolic extract was found to have the highest percentages of phenolic and flavonoid content. Interestingly, ethanolic extract also demonstrated strong DPPH scavenging activity with IC50 at 20.07 ± 0.51µg/mL.


2013 ◽  
Vol 807-809 ◽  
pp. 438-445 ◽  
Author(s):  
Yu Chang Tseng ◽  
Hou Chia Tseng ◽  
Yih Ming Weng

Okara protein isolate was hydrolyzed by two stages enzyme hydrolysis (Protamex+Flavourzyme, Pro+Fla ) and further separated by sequential ultrafiltration (UF) to four fractions (P1~P4). The 2, 2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) scavenging activity of the P3 fraction (1kDa < MW < 3kDa) is 24.6 mmol trolox equivalent (TE)/g peptide and the inhibitory activity is 84.2% at 10 mg/mL. The hydroxyl radical scavenging activity is 85.4% at the same concentration. Pro+Fla-P3 was incorporated into ground beef to determine their effect on lipid oxidation during a 15-day storage period. Pro+Fla-P3 fraction at 500 μg/g significantly inhibited lipid oxidation by 20.8% and 18.2% at day 8 and 15 of storage. The concentration at 250 μg/g could not significantly inhibit lipid oxidation at 15 day. It suggests that okara protein hydrolysates could be developed and used to improve shelf-life of meat products.


Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1241 ◽  
Author(s):  
Jennifer Kusumah ◽  
Luis M. Real Hernandez ◽  
Elvira Gonzalez de Mejia

The objective of this study was to investigate the biochemical antioxidant potential of peptides derived from enzymatically hydrolyzed mung bean (Vigna radiata) albumins using an 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging assay, a ferrous ion chelating assay and an oxygen radical absorbance capacity (ORAC) assay. Peeled raw mung bean was ground into flour and mixed with buffer (pH 8.3, 1:20 w/v ratio) before being stirred, then filtered using 3 kDa and 30 kDa molecular weight cut-off (MWCO) centrifugal filters to obtain albumin fraction. The albumin fraction then underwent enzymatic hydrolysis using either gastrointestinal enzymes (pepsin and pancreatin) or thermolysin. Peptides in the hydrolysates were sequenced. The peptides showed low ABTS radical-scavenging activity (90–100 μg ascorbic acid equivalent/mL) but high ferrous ion chelating activity (1400–1500 μg EDTA equivalent/mL) and ORAC values (>120 μM Trolox equivalent). The ferrous ion chelating activity was enzyme- and hydrolysis time-dependent. For thermolysin hydrolysis, there was a drastic increase in ferrous ion chelating activity from t = 0 (886.9 μg EDTA equivalent/mL) to t = 5 min (1559.1 μg EDTA equivalent/mL) before plateauing. For pepsin–pancreatin hydrolysis, there was a drastic decrease from t = 0 (878.3 μg EDTA equivalent/mL) to t = 15 (138.0 μg EDTA equivalent/mL) after pepsin was added, but this increased from t = 0 (131.1 μg EDTA equivalent/mL) to t = 15 (1439.2 μg EDTA equivalent/mL) after pancreatin was added. There was no significant change in ABTS radical scavenging activity or ORAC values throughout different hydrolysis times for either the thermolysin or pepsin–pancreatin hydrolysis. Overall, mung bean hydrolysates produced peptides with high potential antioxidant capacity, being particularly effective ferrous ion chelators. Other antioxidant assays that use cellular lines should be performed to measure antioxidant capacity before animal and human studies.


2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Santiago Gallegos Tintoré ◽  
Cristina Torres Fuentes ◽  
Javier Solorza Feria ◽  
Manuel Alaiz ◽  
Julio Girón Calle ◽  
...  

The antioxidant and metal chelating activities inJ. curcasprotein hydrolysates have been determined. The hydrolysates were produced by treatment of a nontoxic genotype with the digestive enzymes pepsin and pancreatin and then were characterized by fast protein liquid chromatography and reverse phase chromatography. Peptidic fractions with higher radical scavenging activity were analysed by matrix-assisted laser desorption/ionization mass spectrometry. The antioxidant activity was determined by measuring inhibition of the oxidative degradation ofβ-carotene and by measuring the reactive oxygen species (ROS) in Caco-2 cell cultures. Cu2+and Fe2+chelating activities were also determined. The hydrolysates inhibited the degradation ofβ-carotene and the formation of ROS in Caco-2 cells. The lower molecular weight peptidic fractions from FPLC had stronger antioxidant activity in cell cultures compared with the hydrolysates, which correlated with a higher content in antioxidant and chelating amino acids. These fractions were characterized by a large presence of peptides with different molecular masses. The hydrolysates exhibited both Cu2+and Fe2+chelating activity. It was concluded thatJ. curcasis a good source of antioxidant and metal chelating peptides, which may have a positive impact on the economic value of this crop, as a potential source of food functional components.


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