scholarly journals Optimization of Enzymatic Hydrolysis by Alcalase and Flavourzyme To Enhance the Antioxidant Properties of Jasmine Rice Bran Protein Hydrolysate

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.

2016 ◽  
Vol 69 ◽  
pp. 329-335 ◽  
Author(s):  
Parichart Thamnarathip ◽  
Kamolwan Jangchud ◽  
Sunee Nitisinprasert ◽  
Bongkosh Vardhanabhuti

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.


2011 ◽  
Vol 396-398 ◽  
pp. 1341-1348 ◽  
Author(s):  
Yan Yan Wu ◽  
Lai Hao Li ◽  
Zhen Hua Duan ◽  
Xian Qing Yang ◽  
Jun Shang ◽  
...  

The high antioxidant activity product was isolated from Pinctada fucata muscle by a method of Alcalase hydrolysis. Optimization using response surface methodology was performed and 3D response surfaces were plotted from the mathematical model. The results indicated that the optimal extraction conditions were as follows: pH 7.0, temperature 61°C, E/S 3.01%, hydrolysis time 3h, under the conditions of hydrolysis products of the DPPH radical scavenging rate of 67.3% and the degree of hydrolysis of 31.2%, which was in good agreement with the predicted model value.


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.


Author(s):  
Danielle Maria Fernandes do Prado ◽  
Adrielle Borges de Almeida ◽  
Josemar Gonçalves Oliveira Filho ◽  
Cassia Cristina Fernandes Alves ◽  
Mariana Buranelo Egea ◽  
...  

Background: Food proteins have benefits for human health, which justifies their production and use. In this context, we highlight the use of seeds and byproduct that would be otherwise discarded to produce protein extracts and hydrolyzed proteins generating opportunities to reduce environmental impacts Objective: This work aimed to use different extraction methods to obtain protein extracts from seeds (corn, sorghum, sunflower) and sunflower byproduct to determine their antioxidant activity, and apply different proteolytic enzymes in the hydrolysis of sunflower byproduct Method: The seeds of corn, sorghum, and sunflower, and sunflower byproduct were ground to produce flour and the protein extracts were prepared using five different methods. The bioactivity of fractions was analyzed by different methods (ABTS, DPPH, and FRAP) to evaluate antioxidant activity Results: The most effective methods, which resulted in higher protein extraction and antioxidant activity, were those in which NH4HCO3 (5 mM, pH 8.0) and H2O/C2H6O (2:3) were used in the extraction. The highest protein contents were 797.9, 303.8, and 11296.5 μg/g, and the highest antioxidant activity was 34417.5, 9732.6, and 47473.1 μg TE/g from Soxhlet and Bligh and Dyer defatted extractions for sunflower seed, and sunflower byproduct, respectively. Regarding enzymatic hydrolysis, sunflower byproduct was the substrate that presented the highest degree of hydrolysis (11.06%) when Neutrase® enzyme was used. Enzymatic hydrolysis increased antioxidant activity in the hydrolyzed proteins, approximately 20.0% using Neutrase® and 22.3% using Flavourzyme® treatments. Conclusion: The protein extracts and the hydrolyzed proteins exhibited high antioxidant activity, demonstrating great potential for use as natural antioxidants in food systems


2017 ◽  
Vol 189 (2) ◽  
pp. 192-203
Author(s):  
Ekaterina P. Karaulova ◽  
Anna I. Chepkasova

Peptides extracted from tissues of 11 shellfish species ( Corbicula japonica, Mercenaria stimpsoni, Anadara broughtoni, Patinopecten yessoesis, Crenomytilus grayanus, Spisula sachalinensis, Maktra chinensis, Serripes groenlandicus, Glycymeris yessoensis, Callista brevisiphonata, Dosinia japonica ) are tested for their antioxidant properties in different in vitro conditions. Frozen muscles and viscera of the shellfish were minced and subjected to water extraction of proteins and to hydrolysis with Protamex 1.5 MG. The peptides antioxidant activity was evaluated by assessing of 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity on free radicals generated in oxidative systems. In the experiment, the high perfomance liquid chromatography (HPLC) system (Agilent Technologies 1260) included the frame TSKgel G 3000PWXL, the flow rate was 0.1 mL/min (0.1 N NaCI-20 mM Tris-HCI, pH 8.0), the detection was made under 280 nm. Molecular weight of the proteins was determined by comparison of their retention time with pure protein standards. The enzyme activity was high in conditions of pH in the range of 5.5-8.0, with the maximum under pH 7.0. Among 11 shellfish species, the highest antioxidant activity in water extract was observed for C. japonica , M. stimpsoni , C. brevisiphonata , G. yessoensis , and C. grayanus : 86.3, 68.7, 72.3, 90.2, and 67.5 mg of ascorbic acid/g, respectively. The DPPH radical scavenging activity increased with increasing of the hydrolysis degree. The 1-step hydrolysis with Protamex enhanced the DPPH scavenging activity for all samples, with the highest value for the protein hydrolysate of M. stimpsoni tissues (215 mg of ascorbic acid/g). Size of generated peptides is important for the antioxidant activity therefore molecular weight distribution of the peptides during the proteolysis was investigated using HPLC. Portion of the low molecular weight peptides (≤ 1 kDa) in the protein hydrolysate was increased in 4-14 % as compared with the starting protein. The antioxidant activity correlated positively with the number of low molecular weight peptides in protein hydrolysates.


Author(s):  
E. I. Melnikova ◽  
E. V. Bogdanova ◽  
Y. A. Korneeva

Whey proteins has the highest biological value among all proteins, but the main disadvantage of their use in food technologies is the presence of antigenic epitopes in the molecules that can cause allergic reactions in the human body. The most efficient way to reduce the allergenicity of whey proteins is their enzymatic hydrolysis, which leads to the destruction of antigenic sites and the release of biologically active peptides, including those with antioxidant effects. The purpose of the research is the determination of the whey proteins hydrolysis efficiency in an ultrafiltration concentrate (UF-concentrate) of cheese whey to reduce its allergenicity, as well as to establish the antioxidant activity of the obtained hydrolysate. The experimental studies were carried out at the Core Facilities Centre "Structural and Functional Research of Proteins and RNA" at the FSBSI "Institute of Protein of the Russian Academy of Sciences", as well as "Control and Management of Energy-efficient Projects" at FSBEI HE VSUET. Evaluation of the effectiveness of exposure to whey proteins in the UF-concentrate of cheese whey was carried out by the molecular weight distribution, length and charge of hydrolysis products. ?-lactoglobulin’s derivatives containing from 5 to 17 amino acid residues with a molecular weight of 561 to 1943 Da were found in the finishing hydrolysate. At the same time, hydrolysis made it possible to increase the mass fraction of short-chain peptides, including those with antioxidant properties. As a result of the whey proteins proteolysis in the UF-concentrate of cheese whey, its antioxidant activity increased by 2 times. The degree of hydrolysis of the main allergenic protein, ?-lactoglobulin, was 90-91%. The obtained hydrolysate of whey proteins can be recommended for use in the technology of various assortment groups of dairy products for dietary food with reduced allergenicity and antioxidant effect.


2014 ◽  
Vol 11 (1) ◽  
pp. 29
Author(s):  
Nonnah Ismail ◽  
Juliana Mahmod ◽  
Awatif Khairul Fatihin Mustafa Kamal

In this study, Hydrolysate from angelwing clam (Pholas orientalis) was produced at 0, 1, 2 and 3 hrs and E/S ratio of0.5 and 3%using alcalase where the pH and temperature were kept constant at pH 8.5 and 60°C, respectively. The hydrolysates were analysed for antioxidant and functional properties such as solubility, emulsifying properties and water and oil holding capacity. Degree of hydrolysis (DH), yield, functional and antioxidant properties were influenced by the hydrolysis time and E/S ratio. Higher enzyme concentration (E/S 3%) and longer hydrolysis time increased the DH. Yield was higher at E/S 3% but reduced with hydrolysis time. Longer hydrolysis time produced more soluble hydrolysate and higher metal chelating activity but lower in emulsifying properties and DPPH activity. Higher enzyme concentration resulted in increase only in solubility and metal chelating activity. This study revealed that enzymatic hydrolysis using alcalase should be performed at shorter hydrolysis time using intermediate concentration of enzyme (E/S between 0.5 to 3%) in order to produce angelwing clam hydrolysate with collectively good functional and antioxidant properties. 


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