scholarly journals Antioxidant activities of snakehead (Channa striata) fish skin: peptides hydrolysis using protease tp2 isolate from swamp plant silage

10.5219/1264 ◽  
2020 ◽  
Vol 14 ◽  
pp. 379-384
Author(s):  
Ace Baehaki ◽  
Indah Widiastuti ◽  
Citra Nainggolan ◽  
Nuni Gofar

The purpose of this research was to study the antioxidants activities of peptides from skin fish of snakehead (Channa striata), using hydrolysis of protease TP2 isolate from swamp plant silage. This research 5 treatments hydrolysis time (0, 30, 60, 90, 120 min, respectively), with two replicates, which included several stages of preparation and pre-treatment of the snakehead fish skin production of protease enzymes which were isolated from swamp water, preparation of protein hydrolysates, measurement of hydrolysis degrees, analysis of peptides content and analysis of the antioxidant activity. Results showed that the treatment had given a significant effect on the 5% level of the degree of hydrolysis production (13.98% ”“ 27.08%), with peptides content of 2.73% ”“ 3.78% and antioxidant activity (10.75% ”“ 20.7%). The results of the degree of hydrolysis indicate that the longer the hydrolysis time, the percent degree of hydrolysis will increase. Peptide content and antioxidant activity were increased with increasing hydrolysis time.

2014 ◽  
Vol 707 ◽  
pp. 149-153 ◽  
Author(s):  
Xiao Hu ◽  
Xian Qing Yang ◽  
Lai Hao Li ◽  
Yan Yan Wu ◽  
Wan Ling Lin ◽  
...  

Microalgae protein hydrolysates (MPH) were obtained by enzymatic hydrolysis of defatted microalgae meal using neutral protease. The protein recovery, degree of hydrolysis, and the antioxidant activities of the hydrolysates were investigated. The results demonstrated that hydrolysates prepared by neutral protease at 50 °C for 4 h exhibited the strongest antioxidant activity. Under these conditions, the 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydroxyl radical scavenging activity and the reducing power of the hydrolysates were 68.3%, 50.8% and 1.303, respectively.


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.


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.


Jurnal Kimia ◽  
2020 ◽  
pp. 206
Author(s):  
N. M. Puspawati ◽  
P. P. Dewi ◽  
N. W. Bogoriani ◽  
N. K. Ariati

Penelitian ini bertujuan untuk menentukan aktivitas antioksidan hidrolisat protein yang dihasilkan dari proses hidrolisis enzimatik protein kulit ayam dengan menggunakan variasi konsentrasi enzim papain. Proses hidrolisis dilakukan dengan variasi konsentrasi enzim 1, 3,dan 5% (b/b protein), pada pH 7, suhu 50oC dan waktu hidrolisis 24 jam. Parameter yang diukur meliputi derajat hidrolisis, persen peredaman radikal DPPH (diphenylpicryl hidrazyl), dan komposisi asam amino hidrolisat protein yang paling aktif antioksidan.  Hasil penelitian menunjukkan penggunaan konsentrasi enzim yang berbeda menghasikan hidrolisat protein dengan derajat hidrolisis dan persen peredaman DPPH yang berbeda.  Penggunaan konsentrasi enzim papain 1, 3, dan 5% menghasilkan hidrolisat protein dengan derajat hidrolisis berturut-turut sebesar 9,3±1,8, 18,09±5,6, dan 23,15±6.33%, dan persentase hambatan radikal DPPH pada konsentrasi uji 100 ppm berturut-turut sebesar 16,75±0,07, 58,35±0,00, dan 52,99±0,07%. Hidrolisat protein yang diperoleh menggunakan enzim papain 3% (b/b protein) menunjukkan persen peredaman tertinggi dengan nilai IC50 92,98 ppm, memiliki komposisi asam amino tertiggi asam glutamat dan terendah valine. Kata kunci: antioksidan, enzim papain, hidrolisat protein, kulit ayam This study aimed to determine the antioxidant activity of protein hydrolyzate produced from the enzymatic hydrolysis of chicken skin protein by using variations of the enzyme papain concentration. The hydrolysis process was carried out with variations in the concentration of the enzymes 1, 3, and 5% (w/w protein base), at pH 7, temperature 50oC, and hydrolysis time 24 hours. The parameters measured including degree of hydrolysis, percentage of inhibition of DPPH radical (diphenylpicryl hydrazyl) and amino acid composition of the protein hydrolyzate with the highest antioxidant activity. The results showed that the use of different enzyme concentrations resulted in protein hydrolyzate with different degrees of hydrolysis and percentage of inhibition of DPPH. The use of papain enzymes 1, 3, and 5% produced protein hydrolyzate with the degree of hydrolysis of 9.3 ± 1.8, 18.09 ± 5.6, and 23.15 ± 6.33%, and the percentage of inhibition of DPPH radical at a concentration of 100 ppm 16.75 ± 0.07,  58.35 ± 0.00, and 52.99 ± 0.07% respectively. Protein hydrolyzate obtained using the enzyme papain 3% (w/w protein) exhibited the highest percentage of inhibition of DPPH with an IC50 value of 92.98 ppm, having the highest amino acid composition of glutamic acid and the lowest valine. Keywords: antioxidant, enzyme papain, protein hydrolyzate, chicken skin


Author(s):  
Vitor Geniselli da Silva ◽  
Ruann Janser Soares de Castro

Aiming to explore the use of ionic liquids (ILs) not yet described in the literature, this work evaluated the hydrolysis of proteins from chicken viscera using the protease Alcalase modified and unmodified by the IL tetramethylammonium bromide. The protein hydrolysates produced in the presence of the IL presented values of antioxidant activities 40% higher than the hydrolysates obtained without IL. In addition, with the presence of the IL, it was possible to obtain protein hydrolysates from chicken viscera with similar antioxidant activities, compared to the protein hydrolysates produced without IL, using 1/3 of the amount of enzyme.


2011 ◽  
Vol 20 (No. 1) ◽  
pp. 7-14 ◽  
Author(s):  
M. Hrčková ◽  
M. Rusňáková ◽  
J. Zemanovič

Commercial defatted soy flour (DSF) was dispersed in distilled water at pH 7 to prepare 5% aqueous dispersion. Soy protein hydrolysates (SPH) were obtained by enzymatic hydrolysis of the DSF using three different proteases (Flavourzyme 1000 L, No-vozym FM 2.0 L and Alcalase 2.4 L FG). The highest degree of hydrolysis (DH 39.5) was observed in the presence of protease Flavourzyme. SPH were used for measuring functional properties (foaming stability, gelation). Treatment with Flavourzyme improved foaming of proteins of DSF. Foaming stability was low in the presence of Novozym. Proteases treated DSF showed good gelation properties, mainly in the case of treatment with Flavourzyme. SDS-PAGE analysis showed that after enzyme ad-dition to the 5% aqueous dispersion of DSF each enzyme degraded both b-conglycinin and glycinin. In general, the basic polypeptide from glycinin showed the highest resistance to proteolytic activity. The most abundant free amino acids in the hydrolysates were histidine (30%), leucine (24%) and tyrosine (19%) in the case of the treatment with proteases Alcalase and Novozym, and arginine (22.1%), leucine (10.6%) and phenylalanine (12.9%) in the case of the treatment with Flavourzyme.  


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.


2012 ◽  
pp. 33-41 ◽  
Author(s):  
Zorica Knezevic-Jugovic ◽  
Andrea Stefanovic ◽  
Milena Zuza ◽  
Stoja Milovanovic ◽  
Sonja Jakovetic ◽  
...  

The objectives of this study were to examine the effect of sonication and high-pressure carbon dioxide processing on proteolytic hydrolysis of egg white proteins and antioxidant activity of the obtained hydrolysates. It appeared that the ultrasound pretreatment resulted in an increase in the degree of hydrolysis of the enzymatic reaction while the high-pressure carbon dioxide processing showed an inhibition effect on the enzymatic hydrolysis of egg white proteins to some extent. The antioxidant activity of the obtained hydrolysates was improved by ultrasound pretreatment of egg white proteins at the pH 8.3. Thus, the combination of ultrasound pretreatment at the pH 8.3 and subsequent enzymatic hydrolysis with alcalase at 50?C and pH 8.0 could offer a new approach to the improvement of the functional properties of egg white proteins and their biological activity.


2018 ◽  
Vol 54 (4A) ◽  
pp. 181
Author(s):  
Nguyen Thi Thanh Ngoc

The yield of proteolylic hydrolysis for spent brewer’s yeast by protease and aminoacid contents of hydrolysates (the main  factors influencing in taste of hydrolysed product) depends on factors influencing in catalytic activities of enzymes as temperature, pH value, type of used  enzymes and ratio enzyme/substrate. With the purpose to hydrolyse the spent brewer’s yeast for food application, bitterness of hydrolysate takes the firth consideration, and than the yield of hydrolysing process plays economic role. In this paper, it is dealt with determination of optimal conditions to obtain the highest yield of hydrolysis process and the lowest bitterness of hydrolysate (the bitterness is determined by sensory evaluation, expressed equivalently with concentration of quinine). Response surface methodology (RSM) was used to determine optimum condition for batch proteolytic hydrolysis of spent brewer’s yeast. The influencing factors were investigated as temperature (X1): 40 oC–60 oC; pH (X2): 6.0–9.0, ratio E (flavourzyme)/S (X3): 5–10 U/g and hydrolysis time (X4): 6–9 hours. The experimental responses including degree of hydrolysis (Y1) (%) and bitterness of hydrolysate (Y2) (μmol quinine/ml) are performed in second-degree model. The optimal conditions for obtaining high degree of hydrolysis and low bitterness are determined: Ratio of enzyme mixture (alcalase 7.5 U/g and flavourzyme 8.5 U/g), pH 7.5, hydrolysis temperature at 52oC and hydrolysis time 9 hours. Under the optimal conditions, the actual values obtained for the yield of hydrolysis was 40.81  ± 0.044 % and the bitterness equivalently with concentration of quinine was 16.37 ± 0.03 μmol quinine/ml.


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