scholarly journals Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins

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.

2020 ◽  
Vol 21 (12) ◽  
pp. 1249-1258
Author(s):  
Cindy T. Sepúlveda ◽  
José E. Zapata

Background: Fish is an essential source of nutrients for human nutrition due to the composition of proteins, vitamins, and minerals, among other nutrients. Enzymatic hydrolysis represents an alternative for the use of by-products of the aquaculture industry. Objective: We propose to evaluate the effect of stirring speed, temperature, and initial protein concentration on the degree of hydrolysis of proteins and antioxidant activity of red tilapia (Oreochromis spp.) viscera hydrolysates. Methods: The effect of stirring speed, temperature, and initial protein concentration on the degree of hydrolysis of proteins and antioxidant activity was evaluated using an experimental design that was adjusted to a polynomial equation. The hydrolysate was fractioned to determine the antioxidant activity of the fractions, and functional properties were also measured. Results: Stirring speed and protein concentration presented a statistically significant effect (p <0.05) on all the response variables. However, the temperature did not present a statistically significant effect on the degree of hydrolysis. Discussion: The best conditions of hydrolysis were stirring speed of 51.44 rpm, a temperature of 59.15°C, and the protein concentration of 10 g L-1. The solubility of the hydrolysate protein was high at different pH, and the hydrolysate fraction with the highest antioxidant activity has a molecular weight <1 kDa. Conclusion: The degree of hydrolysis and the biological activity of red tilapia viscera hydrolysates (Oreochromis spp.) are affected by temperature, substrate concentration, and stirring speed. The optimal conditions of hydrolysis allowed to obtain a hydrolysate with antioxidant activity are due to the peptides with low molecular weight.


2018 ◽  
Vol 21 (3) ◽  
pp. 522 ◽  
Author(s):  
Dewi Mutamimah ◽  
Bustami Ibrahim ◽  
Wini Trilaksani

Tuna (Thunnus sp.) by-products from frozen loin and canning industry especially the eye is rich in proteins and in lipids consisting of polyunsaturated fatty acids (PUFA). That requires protective agent (antioxidant) to inhibit the oxidation naturally present and predicted to be protein peptides. Enzymatic hydrolysis of protein is an appropriate method to produce bioactive peptide with such nutraceutical/pharmaceutical function such as an antioxidant peptide. This study aimed to produce protein hydrolysate having a function as anwith an antioxidant activity from eye of tuna through enzymatic hydrolysis and determining the antioxidant activity by DPPH methods. Protein soluble content of tuna’s eye protein hydrolysate (TEPH) ranged from 59.98±0.130 to 94.90±0.002%. The degree of hydrolysis (DH) of TEPH was about 9.10±0.28 to 16.14±0.09%. The highest inhibition of DPPH radical scavenging activity was 93.57±0.05% (at 5 mg/mL) was obtained with a DH of 11.35±0.002% at the concentration 0.1% of papain for 6 hours hydrolysis. The IC50 value of was 1.08±0.008 mg/mL


2018 ◽  
Vol 48 (3) ◽  
Author(s):  
Alessandra Roseline Vidal ◽  
Carine da Fonseca Cechin ◽  
Rogério Luis Cansian ◽  
Renius de Oliveira Mello ◽  
Michele Mantelli Schmidt ◽  
...  

ABSTRACT: Enzymatic hydrolysis (pepsin) assisted with or without ultrasound in the functional properties of hydrolyzates from different collagens were analyzed. Degree of hydrolysis, antioxidant activity (DPPH) and antimicrobial activity (MIC) were assessed. The treatment that resulted in greater antioxidant activity for the fiber sample was with the use of 4% of enzyme and concomitant ultrasound (40.7%), leading to a degree of hydrolysis of 21.7%. For the powdered fiber sample the hydrolysis treatment with use of 4% of enzyme resulted in lower protein content (6.97mg/mL), higher degree of hydrolysis (19.9%) and greater antioxidant activity (38.6%). The hydrolyzates showed inhibitory capacity against gram-negative bacteria Salmonella choleraesuis and gram-positive bacteria Staphylococcus aureus. It can be concluded that enzymatic hydrolysis concomitant or not with the use of ultrasound increased the functionality of the fiber and powdered fiber samples, for the other samples its use as supplementary treatment was not productive, due to the worse results of antioxidant activity (DPPH) reported. However, it provided greater hydrolysis degree.


1935 ◽  
Vol 109 (1) ◽  
pp. 169-175
Author(s):  
Essie White Cohn ◽  
Abraham White

2013 ◽  
Vol 411-414 ◽  
pp. 3205-3209
Author(s):  
Fang Qian ◽  
Lei Zhao ◽  
Shu Juan Jiang ◽  
Guang Qing Mu

Based on single factor analysis for the enzymatic hydrolysis of whey protein, papain was selected as the optimal enzyme and its enzymatic hydrolysis conditions were optimized by the quadratic regression orthogonal rotary test. The orthogonal regression model for degree of hydrolysis (DH) to three factors including temperature (X1), time (X2), enzyme dosage (X3) was established as follow: DH=10.40+0.22X1+0.30X2+1.31X3+0.019X1X2+0.011X1X3-0.039X2X3-0.39X12-0.16X22-0.40X32, Verification test showed a DH of 11.7% was obtained at the optimal hydrolysis condition of 56.6°C, 113.8 min and enzyme 8213.7 U /g protein, which basically consisted with the model theoretical value.


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. &nbsp;


Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1312
Author(s):  
Pei-Gee Yap ◽  
Chee-Yuen Gan

Active fragments (bioactive peptides) from the chicken egg white proteins were expected to exert tyrosinase inhibitory activities in which skin hyperpigmentation could be prevented. Egg white was hydrolyzed by trypsin, chymotrypsin and the combination of both enzymes. The enzyme treatments achieved >50% degree of hydrolysis (DH) at substrate-to-enzyme (S/E) ratio of 10–30 (w/w) and hydrolysis time of 2–5 h. A crossed D-optimal experimental design was then used to determine the optimal enzyme composition, S/E ratio and hydrolysis time in order to yield hydrolysates with strong monophenolase and diphenolase inhibitory activities. The optimized conditions 55% trypsin, 45% chymotrypsin, S/E 10:1 w/w and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 w/w and 3.18 h achieved 48.1% diphenolase activity inhibition. LC/MS and MS/MS analyses identified the peptide sequences and the subsequent screening had identified 7 peptides (ILELPFASGDLLML, GYSLGNWVCAAK, YFGYTGALRCLV, HIATNAVLFFGR, FMMFESQNKDLLFK, SGALHCLK and YFGYTGALR) as the potential inhibitor peptides. These peptides were able to bind to H85, H94, H259, H263, and H296 (hotspots for active residues) as well as F92, M280 and F292 (stabilizing residues) of tyrosinase based on structure-activity relationship analysis. These findings demonstrated the potential of egg white-derived bioactive peptides as skin health therapy.


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