scholarly journals Protein Hydrolysate from Pterygoplichthys disjunctivus, Armoured Catfish, with High Antioxidant Activity

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1628 ◽  
Author(s):  
Yuchen Guo ◽  
Nicholas Michael ◽  
Jorge Fonseca Madrigal ◽  
Carlos Sosa Aguirre ◽  
Paula Jauregi

Pterygoplichthys disjunctivus, locally named the armoured catfish, is a by-catch of tilapia fishing that accounts for up to 80% of total captured fish in the Adolfo Lopez Mateos dam, in Michoacán, México, affecting the economy of its surrounding communities. This invasive fish is discarded by fishermen since native people do not consume it, partly due to its appearance, yet it is rich in protein. The aim of this study was to produce hydrolysates from armoured catfish using food-grade proteases (neutrases HT and PF and alcalase PAL) and investigate the processing conditions (pH and temperature) that lead to a high degree of hydrolysis, antioxidant activity, and Angiotensin I-Converting Enzyme (ACE) Inhibitory activity. No other similar research has been reported on this underutilized fish. The antioxidant activity was measured by three different methods, ABTS, FRAP and ORAC, with relevance to food and biological systems in order to obtain a more comprehensive assessment of the activity. In addition, the main peptide sequences were identified. All enzymes produced hydrolysates with high antioxidant activity. In particular, the protease HT led to the highest antioxidant activity according to the ABTS (174.68 μmol Trolox equivalent/g fish) and FRAP (7.59 mg ascorbic acid equivalent/g fish) methods and almost the same as PAL according to the ORAC method (51.43 μmol Trolox equivalent/g fish). Moreover, maximum activity was obtained at mild pH and temperature (7.5; 50 °C). Interestingly, the ORAC values obtained here were higher than others previously reported for fish hydrolysates and similar to those reported for fruits such as blueberries, apples and oranges. The peptide sequence IEE(E) was present in several peptides in both hydrolysates; this sequence may be partly responsible for the high antioxidant activity, particularly the one based on iron-reducing power. These findings will be relevant to the valorization of other fish/fish muscle discards and could contribute to the production of food supplements and nutraceuticals.

2021 ◽  
Author(s):  
Kanrawee Hunsakul ◽  
Thunnop Laokuldilok ◽  
Vinyoo Sakdatorn ◽  
Wannaporn Klangpetch ◽  
Niramon Utama-ang

Abstract This study aimed to optimize the hydrolysis conditions for producing jasmine rice bran protein hydrolysate (JBH) using response surface methodology (RSM). The independent variables were the ratio of flavourzyme to alcalase (Fl: Al; 0: 100 to 15: 85; 2.84% enzyme concentration) and hydrolysis time (60–540 min). The optimum hydrolysate was obtained at an Fl: Al ratio of 9.81: 90.19 for 60 min, since it enabled high amounts of protein, high antioxidant activity and more low molecular weight proteins. The experimental values obtained were a degree of hydrolysis (DH) of 7.18%, a protein content of 41.73%, an IC50 for DPPH of 6.59 mg/mL, an IC50 for ABTS of 0.99 mg/mL, FRAP of 724.81 mmol FeSO4/100 g, and 322.35 and 479.05 mAU*s for peptides with a molecular weight of <3 and 3–5 kDa, respectively. Using a mixture of enzymes revealed the potential of mixed enzymes to produce JBH containing more small peptides and high antioxidant activity.


2012 ◽  
Vol 554-556 ◽  
pp. 891-899
Author(s):  
Xu Yan Zong ◽  
Li Li ◽  
Xu Qiao Feng ◽  
Hui Bo Luo ◽  
Jian Zhou ◽  
...  

Brewer’s spent grain (BSG) protein extracted from BSG was hydrolyzed using Alcalase to produce BSG protein hydrolysate. BSG protein hydrolysate was fractionated by ultrafiltration to obtain brown color BSG peptides. Antioxidant activity of BSG peptides was analyzeded and compared with reduced glutathione (GSH). BSG peptides exhibited 50% of scavenging activities on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, hydroxyl radical, and superoxide radical with concentrations less than 0.8 mg/mL, 0.6 mg/mL and 0.6 mg/mL, respectively. The reducing power of BSG peptides was 0.70 at the concentration of 2.00 mg/mL. 86.30% of the total amount of the BSG peptides purified by gel permeation chromatography was below 2000 Da. Because of its antioxidant activity, stability, nutritive value and low cost, BSG peptides exerts a possibility to use in food or cosmetic products.


PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e8297 ◽  
Author(s):  
Asep A. Prihanto ◽  
Rahmi Nurdiani ◽  
Annas D. Bagus

Background Fish byproducts are commonly recognized as low-value resources. In order to increase the value, fish byproducts need to be converted into new products with high functionality such as fish protein hydrolysate (FPH). In this study, FPH manufactured from parrotfish (Chlorurus sordidus) heads using different pH, time and sample ratio was investigated. Methods Hydrolysis reactions were conducted under different pHs (5, 7, and 9) and over different durations (12 and 24 h). Control treatment (without pH adjustment (pH 6.4)) and 0 h hydrolsisis duration were applied. Hydrolysates were characterized with respect to proximate composition, amino acid profile, and molecular weight distribution. The antioxidant activity of the hydrolysate was also observed. Results The pH and duration of hydrolysis significantly affected (p < 0.05) the characteristics of FPH. The highest yield of hydrolysate (49.04 ± 0.90%), with a degree of hydrolysis of 30.65 ± 1.82%, was obtained at pH 9 after 24 h incubation. In addition, the FPH had high antioxidant activity (58.20 ± 0.55%), with a high level of essential amino acids. Results suggested that FPH produced using endogenous enzymes represents a promising additive for food and industrial applications.


Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 833
Author(s):  
Xiaogang Zhang ◽  
Parinya Noisa ◽  
Jirawat Yongsawatdigul

Production of protein hydrolysate as nutraceuticals is typically based on the activity of the hydrolysate, which might not yield the optimal activity under physiological condition due to structural modification of peptides upon gastrointestinal (GI) digestion. This study systematically compared the chemical and cellular antioxidant activities of the in vitro digesta of tilapia protein and its hydrolysates prepared with various degree of hydrolysis (DH) by Alcalase. The enzymes used in the in vitro GI digestion analysis significantly contributed to the peptide content, Trolox equivalent antioxidant capacity (TEAC), and oxygen radical absorbance capacity (ORAC). Proteins and all hydrolysates were slightly digested by pepsin but hydrolyzed extensively by pancreatin. Both hydrolysate and digesta predominantly scavenged free radicals via hydrogen atom transfer (HAT). The antioxidant activities of the hydrolysates increased with the increasing DH up to 16 h of hydrolysis. However, the digesta of 10-h hydrolysate displayed the highest chemical and HepG2 cellular antioxidant activities, while the protein digesta displayed the lowest. Principal component analysis (PCA) showed that the TEAC of the digesta was positively correlated with the cellular antioxidant activity (CAA). Therefore, the production of protein hydrolysate should be optimized based on the activity of the hydrolysate digesta rather than that of hydrolysates.


2012 ◽  
Vol 554-556 ◽  
pp. 1327-1331
Author(s):  
Li Jun Zhang ◽  
Qian Cheng Zhao ◽  
Bing Bing Wang ◽  
Xue Wan ◽  
Zhi Bo Li ◽  
...  

Protein hydrolysates from Tuna frame (TFPH) and Pollock frame (PFPH) were prepared by papain, respectively.The yield, the basic composition content, the antioxidant activity and functional properties (solubility, emulsifying and foaming ability) and the degree of hydrolysis of the protein hydrolysates were evaluated. Results suggest that solubility, antioxidant activity of protein hydrolysate from Pollock frame are better than that of tuna frame, but the yield is lower than that of tuna frame.


2013 ◽  
Vol 634-638 ◽  
pp. 1435-1440 ◽  
Author(s):  
Shuai Wang ◽  
Li Cheng Zhong ◽  
Xue Chao Zhai ◽  
Dong Dong Yin ◽  
Xin Yu Wu

Deer blood was hydrolyzed using Alcalase with hydrolysis time ranged form 0 to 6 h, and the degree of hydrolysis (DH) of protein hydrolysates increased with increasing hydrolysis time (P < 0.05). The reducing power, radicals scavenging activities and Cu2+-chelation ability of deer blood hydrolysate (DBH) significantly enhanced with increasing hydrolysis time (P < 0.05). The antioxidant activity of DBH, indicated by thiobarbituric acid-reactive substance (TBARS) values in a liposome-oxidizing system, increased with increasing DH (P < 0.05). The results indicated that antioxidant activity of DBH depended on hydrolysis time, and the hydrolyzed deer blood could be a potent food antioxidant.


2021 ◽  
Vol 302 ◽  
pp. 02010
Author(s):  
Pratchaya Muangrod ◽  
Wiriya Charoenchokpanich ◽  
Vilai Rungsardthong ◽  
Savitri Vatanyoopaisarn ◽  
Benjamaporn Wonganu ◽  
...  

Edible jellyfish have been consumed as food for more than a century with offering high protein and crunchy texture. The pepsin hydrolysis of jellyfish protein yields jellyfish protein hydrolysate (ep-JPH), reported for potential bioactivities such as antioxidant activity or antihypertensive activities. Due to the substantial number of by-products generated from jellyfish processing, the by-products were then selected as a raw material of JPH production. This research aimed to evaluate the effect of the hydrolysis time of pepsin on the antioxidant activity of ep-JPH. The dried desalted jellyfish by-products powder was enzymatically hydrolysed by 5% (w/w) pepsin, and the hydrolysis time was varied from 6, 12, 18, and 24 h at 37oC. Results showed that increased hydrolysis time increased the degree of hydrolysis (DH) and inhibition of DPPH radical. The 24 h ep-JPH possessed the highest DH and the highest inhibitory effect of DPPH radical. The results demonstrated that, in this experiment, all ep-JPHs were DPPH radical scavengers, exhibiting different inhibition activities depending on DH values.


Antioxidants ◽  
2020 ◽  
Vol 9 (1) ◽  
pp. 76 ◽  
Author(s):  
Natividad Chaves ◽  
Antonio Santiago ◽  
Juan Carlos Alías

Plants have a large number of bioactive compounds with high antioxidant activity. Studies for the determination of the antioxidant activity of different plant species could contribute to revealing the value of these species as a source of new antioxidant compounds. There is a large variety of in vitro methods to quantify antioxidant activity, and it is important to select the proper method to determine which species have the highest antioxidant activity. The aim of this work was to verify whether different methods show the same sensitivity and/or capacity to discriminate the antioxidant activity of the extract of different plant species. To that end, we selected 12 species with different content of phenolic compounds. Their extracts were analyzed using the following methods: 2,2-di-phenyl-1-picrylhydrazyl (DPPH) radical scavenging capacity assay, ferric reducing (FRAP) assay, Trolox equivalent antioxidant capacity (ABTS) assay, and reducing power (RP) assay. The four methods selected could quantify the antioxidant capacity of the 12 study species, although there were differences between them. The antioxidant activity values quantified through DPPH and RP were higher than the ones obtained by ABTS and FRAP, and these values varied among species. Thus, the hierarchization or categorization of these species was different depending on the method used. Another difference established between these methods was the sensitivity obtained with each of them. A cluster revealed that RP established the largest number of groups at the shortest distance from the root. Therefore, as it showed the best discrimination of differences and/or similarities between species, RP is considered in this study as the one with the highest sensitivity among the four studied methods. On the other hand, ABTS showed the lowest sensitivity. These results show the importance of selecting the proper antioxidant activity quantification method for establishing a ranking of species based on this parameter.


2021 ◽  
Vol 17 ◽  
Author(s):  
Juliana Latorres ◽  
Wilson Wasielesky Jr ◽  
Carlos Prentice

Background: Aquatic organisms are considered to be an important source of bioactive peptides with a high antioxidant and antihypertensive capacity. Therefore, the objective of this study was to hydrolyse peptide fractions from white shrimp (Litopenaeus vannamei) muscle by Alcalase and Protamex and to evaluate the angiotensin I-converting enzyme (ACE) inhibitory and the antioxidant activities. Methods: Protein hydrolysates of White shrimp were obtained by enzymatic hydrolysis using Alcalase and Protamex until the degree of hydrolysis reached 10% and 20%. Peptide fractions were obtained from White shrimp protein hydrolysates by ultrafiltration using membranes with sizes of 10 and 3 kDa. The antioxidant activity was evaluated for the three peptide fractions (F1: >10 kDa, F2: 3-10 kDa and F3: <3 kDa). To measure the antihypertensive activity, fractions with molecular sizes of less than 3 kDa were used. Results: The fractions obtained with Alcalase showed greater inhibitory effects on the ACE. In general, the molecular weight of the fractions influenced the antioxidant activity, with fractions smaller than 3 kDa having a high capacity for sequestering the DPPH radical, while peptide fractions with a size greater than 10 kDa presented higher reducing power. However, in capturing the ABTS radical, a high antioxidant capacity was observed for both fractions. Conclusion: The results suggest white shrimp would be an attractive raw material for the manufacture of antioxidant and anti-hypertensive nutraceutical ingredients.


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