scholarly journals Protease from Aspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Ruann Janser Soares de Castro ◽  
Helia Harumi Sato

This study reports the biochemical characterization of a protease from Aspergillus oryzae LBA 01 and the study of the antioxidant properties of protein hydrolysates produced with this protease. The biochemical characterization showed that the enzyme was most active over the pH range 5.0–5.5 and was stable from pH 4.5 to 5.5. The optimum temperature range for activity was 55–60°C, and the enzyme was stable at temperatures below 45°C. The activation energy (Ea) for azocasein hydrolysis and temperature quotient (Q10) were found to be 37.98 kJ mol−1 and 1.64–1.53 at temperature range from 30 to 55°C, respectively. The enzyme exhibited t1/2 of 97.63 min and a D value of 324.31 at the optimum temperature for activity (57.2°C). Protease from A. oryzae LBA 01 was shown as a potentially useful biocatalyst for protein hydrolysis, increasing the antioxidant activities of soy protein isolate, bovine whey protein, and egg white protein from 2.0- to 10.0-fold.

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.


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.


2017 ◽  
Vol 7 (7) ◽  
pp. 545 ◽  
Author(s):  
Tolulope Joshua Ashaolu ◽  
Chutha Takahashi Yupanqui

Background: Soy protein isolate (SPI) is increasingly used in foods because it is a high quality non-dairy protein with excellent functional properties. However, soy allergy is one of the world’s major eight food allergies. Objective: To investigate the anti-allergic activity of soy protein hydrolysates (SPHs) produced with alcalase and pepsin proteases.Methods: SPI was enzymatically hydrolysed using the proteases, while evaluating the reaction conditions which include E/S (enzyme to substrate ratio) of 0.5%, 1.0% and 1.5% (250 u/mg and 5 u/g of pepsin and alcalase respectively); and hydrolysis time (0 min, 30 min, 1h, 2h, 4h and 8h). Afterwards, rat basophilic leukaemia (RBL)-2H3 cells activated by the IgE-antigen complex were used to assess mast cell degranulation inhibitory activity of the SPHs by the release of β-hexosaminidase. RBL-2H3 cells were sensitized with monoclonal anti-dinitrophenol (DNP) specific IgE and challenged with the antigen DNP-bovine serum albumin in the presence or absence of SPHs.Results: It was observed that 0.1 mg/mL concentration of the 0.5% E/S SPHs prepared in the first 4h significantly (P < 0.05) inhibited β-hexosaminidase release in an IgE-antigen complex-stimulated RBL-2H3 cells compared to those produced at other time intervals, E/S, and concentrations.Conclusion: This is the first report of its kind that shows the ability of SPHs to suppress degranulation of RBL-2H3 cells. Consequently, SPHs have good prospects to be used as potential sources of low cost hypo or anti-allergic protein.Keywords: Soy Protein Isolate, Soy Protein Hydrolysates, RBL-2H3 Cells, β-Hexosaminidase, Anti-allergy


2016 ◽  
Vol 7 (5) ◽  
pp. 2431-2437 ◽  
Author(s):  
Abimbola K. Arise ◽  
Adeola M. Alashi ◽  
Ifeanyi D. Nwachukwu ◽  
Oluwatosin A. Ijabadeniyi ◽  
Rotimi E. Aluko ◽  
...  

In this study, the bambara protein isolate (BPI) was digested with three proteases (alcalase, trypsin and pepsin), to produce bambara protein hydrolysates (BPHs).


e-Polymers ◽  
2021 ◽  
Vol 21 (1) ◽  
pp. 575-589
Author(s):  
Xin Zhou ◽  
Qingyin Dai ◽  
Xi Huang ◽  
Zhiyong Qin

Abstract The mangosteen peel extract (MPE) was used to obtain soy protein isolate (SPI) films. The results show that MPE exhibited a high content of total phenolics and antioxidant activity. Moreover, the MPE can enhance the antibacterial–antioxidant properties, UV-visible light barrier properties, and water-resistant properties of the SPI films. The presence of MPE resulted in an increase in water vapor permeability and hydrophobicity. The extract addition also reduced the film’s crystallinity along with a decrease in the mechanical property and lowering of the maximum degradation temperature. Attenuated total reflectance Fourier transform infrared spectroscopy revealed that the polyphenols in MPE could interact with SPI through hydrogen bonds and hydrophobic interactions, and the addition of MPE changed the secondary structure of SPI with a decrease in β-sheets and an increase in β-turns and random coils. Scanning electron microscopy showed that all the films exhibited smooth and homogenous morphology on the surface and on some layers through cross-sectional images. Our results suggested that the MPE would be a promising ingredient to make SPI films used as an active packaging material.


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