scholarly journals Enzymatic hydrolysis of extruded soybean meal at high substrate concentrations

2016 ◽  
pp. 63-73
Author(s):  
Anton Sharikov ◽  
Anna Sereda ◽  
Elena Kostyleva ◽  
Irina Velikoretskaya ◽  
Victor Polyakov

Extrusion as a pretreatment before enzymatic hydrolysis of soybean meal is an effective technique to eliminate antinutritional properties of the main thermostable soy proteins glycinin and ?-conglycinin for production of feed ingredients with enhanced properties. In terms of economic efficiency, biotechnological processes are preferable to carry out at high substrate concentrations. The aim of the investigation was to evaluate the influence of high substrate concentrations in the range of 26-32% and enzyme dosages (0.4 - 3.1 PU/g) on efficiency of hydrolysis of extruded toasted soybean meal with bacterial protease. The results showed that maximum degree of hydrolysis was 42.1% at the enzyme dosage of 3.6 PU/g and at the substrate concentration of 29.0%. The increase in the substrate concentration had a strong effect on the deterioration of dynamic viscosity of the hydrolysates from 0.2 to 5.82 Pa?s. A combination of extrusion cooking at 120?C and enzymatic treatment with ?Protolad B? protease enabled hydrolysis of glycinin and ?-conglycinin to peptides with molecular mass below 15 kDa.

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.


2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Yanbin Zheng ◽  
Qiushi Chen ◽  
Anshan Shan ◽  
Hao Zhang

For utilizing the blood cells (BCs) effectively, enzymatic hydrolysis was applied to produce the enzymatically hydrolyzed blood cells (EHBCs) by using a neutral protease as a catalyst. The results of the single-factor experiments showed optimal substrate concentration, enzyme to substrate ratio (E/S), pH, temperature, and incubation period were 1.00%, 0.10, 7.00, 50.00°C, and 12.00 h, respectively. The optimized hydrolysis conditions from response surface methodology (RSM) were pH 6.50, E/S 0.11, temperature 45.00°C, and incubation period 12.00 h. Under these conditions (substrate concentration 1.00%), the degree of hydrolysis (DH) was 35.06%. The free amino acids (FAAs) content of the EHBCs (35.24%) was 40.46 times higher than BCs while the total amino acids (TAAs) content was lower than BCs. The scores of lysine (human 0.87; pig 0.97), valine (human 1.42; pig 1.38), leucine (human 1.50; pig 1.90), tyrosine (human 0.84; pig 1.09), and histidine (human 2.17; pig 2.50) indicated that the EHBCs basically fulfilled the adult human and pig nutritional requirements. The calculated protein efficiency ratios (C-PERs) of the EHBCs were 3.94, 6.19, 21.73, and 2.04. In summary, the EHBCs were produced successfully with optimized conditions and could be a novel protein source for humans and pigs.


2019 ◽  
Vol 15 (2) ◽  
pp. 144-153 ◽  
Author(s):  
Nathalia A. Gómez ◽  
Leidy J. Gómez ◽  
José E. Zapata

Background: The animal blood that is produced in a slaughterhouse is a potential source of inexpensive proteins used in the food industry around the world. However, 60% of it is surplus, and it ends with a negative environmental impact. Introduction: The enzymatic hydrolysis of proteins represents a good way to produce peptides with different biological activities. Methods: Enzymatic hydrolysis of bovine plasma with subtilisin at an alkaline pH and 61.5°C was performed using the pH-stat method. Experiments were conducted considering the effects of a high initial substrate concentration (So) and the enzyme/substrate ratio (E/S) minimizing the processing time necessary to obtain a specific degree of hydrolysis (DH). Results: The best conditions obtained were 42 g/L of So and 0.89 AU/g substrate of E/S until a DH of 20% in 11,1 ± 1,1 min was achieved to the tested conditions, which result in a fitted empirical polynomial equation of degree 3. Conclusion: A kinetic equation is established to relate the DH and the reaction time to a relative error of less than 5% in the fit, to obtain a good antioxidant product in an industrially interesting time. Additionally, the results suggest a good adjustment of the data with a determination coefficient (R2) of 0.9745 in validation.


1987 ◽  
Vol 65 (1) ◽  
pp. 23-29 ◽  
Author(s):  
Sukekuni Mukataka ◽  
Tetsuo Kobayashi ◽  
Seigo Sato ◽  
Joji Takahashi

Molecules ◽  
2019 ◽  
Vol 24 (4) ◽  
pp. 792 ◽  
Author(s):  
Yerko Fredes ◽  
Lesly Chamorro ◽  
Zaida Cabrera

The effects of the reaction medium and substrate concentration were studied on the selectivity of Novozym 435 using the asymmetric hydrolysis of dimethyl-3-phenylglutarate as a model reaction. Results show that the use of choline chloride ChCl:urea/phosphate buffer 50% (v/v) as a reaction medium increased the selectivity of Novozym 435 by 16% (e.e = 88%) with respect to the one in 100% phosphate buffer (e.e = 76%). Best results were obtained when high substrate concentrations (well above the solubility limit, 27-fold) and ChCl:urea/phosphate buffer 50% (v/v) as reaction medium at pH 7 and 30 °C were used. Under such conditions, the R-monoester was produced with an enantiomeric purity of 99%. Novozym 435 was more stable in ChCl:urea/phosphate buffer 50% (v/v) than in phosphate buffer, retaining a 50% of its initial activity after 27 h of incubation at pH 7 and 40 °C. Results suggest that the use of deep eutectic solvents (ChCl:urea/phosphate buffer) in an heterogeneous reaction system (high substrate concentration) is a viable and promising strategy for the synthesis of chiral drugs from highly hydrophobic substrates.


2020 ◽  
pp. 53-61
Author(s):  
Ansharullah Ansharullah ◽  
Muhammad Natsir

The aims of this study were to characterize the kinetics of enzymatic hydrolysis of sago starch, obtained from Southeast Sulawesi Indonesia. The enzyme used for hydrolysis was bacterial ∝-amylase (Termamyl 120L from Bacillus licheniformis, E. C. 3.2.1.1).  The method to determine the initial velocity (Vo) of the hydrolysis was developed by differentiation a nonlinear equation (NLE).  The Vo of the hydrolysis was measured at various pH (6.0, 6.5,and 7.0), temperatures (40, 60, 75 and 95oC), enzyme concentrations (0.5, 1.0, 1.5 and 2.0 µg per mL) and in the presence of 70 ppm Ca++. The optimum conditions of this experiment were found to be at pH 6.5 – 7.0 and 75oC, and the Vo increased with increasing enzyme concentration. The Vo values at various substrate concentrations were also determined, which were then used to calculate the enzymes kinetics constant of the hydrolysis, including Michaelis-Menten constant (Km) and maximum velocity (Vmax) using a Hanes plot.  Km and Vmax values were found to be higher in the measurement at pH 7.0 and 75oC. The Km values  at four  different combinations of pH and temperatures (pH 6.5, 40oC; pH 6.5, 75oC; pH 7.0, 40oC; pH 7.0, 75oC) were found to be 0.86, 3.23, 0.77 and 3.83 mg/mL, respectively; and Vmax values were 17.5, 54.3, 20.3 and 57.1 µg/mL/min, respectively. The results obtained showed that hydrolysis rate of this starch was somewhat low.


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.  


2011 ◽  
Vol 165 (3-4) ◽  
pp. 832-844 ◽  
Author(s):  
Bon-Wook Koo ◽  
Trevor H. Treasure ◽  
Hasan Jameel ◽  
Richard B. Phillips ◽  
Hou-min Chang ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document