scholarly journals Enzymatic hydrolysis of wheat starch for glucose syrup production

DYNA ◽  
2020 ◽  
Vol 87 (214) ◽  
pp. 173-182
Author(s):  
Juan Camilo Acosta Pavas ◽  
Laura Alzate Blandón ◽  
Ángela Adriana Ruiz Colorado

An analysis of the enzymatic hydrolysis of wheat starch was performed. The gelatinization stage was carried out between 90-95°C for 15min. In the liquefaction stage, a commercial α-amylase was used with an enzyme-substrate ratio (E/S ratio) 0.036%w/w at 60°C and pH 5.8 for 4h. In the saccharification stage, a commercial amyloglucosidase was used with an E/S ratio of 0.11% w/w at 60°C and pH 4.3 for 6h. A second hydrolysis was evaluated using a E/S ratio of  0.18%w/w in the saccharification stage. Two methods of enzymatic deactivation, boiling temperatures and pH were evaluated. Inhibitory effects were studied by adding 180g/L of glucose to the process. It is concluded that increases in the E/S ratio decrease reaction times but reaches similar concentrations than lower ratios, the most efficient enzymatic deactivation method is pH. In the inhibition tests, it was determined that there are no glucose inhibitory effects.

2012 ◽  
Vol 554-556 ◽  
pp. 1387-1394
Author(s):  
He Jian Xiong ◽  
Longfei Cao ◽  
Huajun You ◽  
Qingpi Yan ◽  
Ying Ma

Tilapia frames were subjected to enzymatic hydrolysis using Flavouzryme and Papain with a ratio of 2:1. The relationship of temperature (40 to 60°C), enzyme: substrate ratio (0.5% to 4.5%), initial pH (6.0 to 8.0) and hydrolysis time (1h to 9h) to the degree of hydrolysis were determined. The enzymatic hydrolysis was optimized for maximum degree of hydrolysis using surface response methodology. The optimum conditions for enzymatic hydrolysis of tilapia frames were temperature 53°C, enzyme : substrate ratio of 3.5%, initial pH 7.2, and reaction time 7h. Under these conditions a degree of hydrolysis of 40.01% were obtained. The yield of free amino acids in the hydrolysate was 46.61mg/g tilapia frames. The flavor amino acids and essential amino acids occupied up to 31.8% and 49.0% of the total free amino acids respectively. The hydrolysate of waste tilapia frames showed good potential for applications such as protein supplementation in food system.


LWT ◽  
2011 ◽  
Vol 44 (4) ◽  
pp. 1164-1171 ◽  
Author(s):  
MyoungLae Cho ◽  
Jung H. Han ◽  
SangGuan You

1992 ◽  
Vol 3 (5) ◽  
pp. 369-371 ◽  
Author(s):  
Milan Polakovič ◽  
Gabriela Handriková ◽  
Martin Košík

Materials ◽  
2019 ◽  
Vol 12 (9) ◽  
pp. 1465 ◽  
Author(s):  
Mirian Angelene González-Ayón ◽  
Ángel Licea-Claveríe ◽  
José Benigno Valdez-Torres ◽  
Lorenzo A. Picos-Corrales ◽  
Rosabel Vélez-de la Rocha ◽  
...  

This work shows an optimized enzymatic hydrolysis of high molecular weight potato galactan yielding pectic galactan-oligosaccharides (PGOs), where endo-β-1,4-galactanase (galactanase) from Cellvibrio japonicus and Clostridium thermocellum was used. For this, response surface methodology (RSM) by central composite design (CCD) was applied. The parameters varied were temperature (°C), pH, incubation time (min), and enzyme/substrate ratio (U/mg). The optimized conditions for the production of low degree of polymerization (DP) PGOs were obtained for each enzyme by spectrophotometric assay and confirmed by chromatography. The optimal conditions predicted for the use of C. japonicus galactanase to obtain PGOs of DP = 2 were T = 51.8 °C, pH 5, E/S = 0.508 U/mg, and t = 77.5 min. For DP = 3, they were T = 21 °C, pH 9, E/S = 0.484 U/mg, and t = 12.5 min; and for DP = 4, they were T = 21 °C, pH 5, E/S = 0.462 U/mg, and t = 12.5 min. The efficiency results were 51.3% for substrate hydrolysis. C. thermocellum galactanase had a lower yield (35.7%) and optimized conditions predicted for PGOs of DP = 2 were T = 60 °C, pH 5, E/S = 0.525 U/mg, and time = 148 min; DP = 3 were T = 59.7 °C, pH 5, E/S = 0.506 U/mg, and time = 12.5 min; and DP = 4, were T = 34.5 °C, pH 11, E/S = 0.525 U/mg, and time = 222.5 min. Fourier transformed infrared (FT-IR) and nuclear magnetic resonance (NMR) characterizations of PGOs are presented.


1998 ◽  
Vol 4 (2) ◽  
pp. 91-98 ◽  
Author(s):  
F. Mendonça Diniz ◽  
A.M. Martin

Muscle tissue from the spiny dogfish ( Squalus acanthias) was enzymatically hydrolysed using a bacterial endopeptidase. The influence of the process variables (temperature, pH, enzyme/ substrate ratio and reaction time) was investigated with regards to the extent of proteolytic degra dation and the recovery of soluble nitrogen from the substrate. Maximum significant nitrogen recovery (NR) was found to be 76.2%, in a 2 h proteolytic reaction. Optimum conditions were 55 °C, pH 8.0 and an enzyme/substrate ratio of 40 mg enzyme/g minced shark muscle (wet weight basis). Under these conditions, a degree of hydrolysis (DH) of 18.6% was obtained. A linear corre lation ( R2 = 0.99) was found to exist between the two measured parameters, NR and DH.


2018 ◽  
Vol 12 (3) ◽  
Author(s):  
A. Kapustian ◽  
O. Antipina ◽  
R. Budiak

The possibility of obtaining bioavailable mixed ligand chelate complexes of Magnesium has been considered. As bioligands, it is proposed to use the metabolites and products of enzymatic hydrolysis of the peptidoglycans of the cell walls of Bifidobacterium bifidum AC-1670. As ligands, fragments of peptidoglycans of cell walls of bifidobacteria, which have their own immunotropic effects, were used. Destruction of bacterial cells was done by ultrasound treatment with subsequent enzymatic hydrolysis with papain. It was found that the highest content of potential ligands for chelation was obtained by ultrasound treatment at a frequency of 35 kg for 600 seconds with subsequent enzymatic hydrolisys, which lasted for 180 minutes at a ratio of the enzyme: substrate 1:1. In this case, the accumulation of amino acids in the hydrolyzate was 11.35 mg/cm3, low molecular weight peptides - 7.54 mg/cm3. The liquid phase of the product of the disintegration of the bacterial mass is investigated for the presence of metabolites that can participate in the formation of chelating magnesium complexes. Qualitative composition and quantitative content of organic acids are determined. It is established that in the product of disinfection of bifidobacteria the following acids are present: acetic (445.5 mg/dm3), lactic (284.6 mg/dm3), benzoic (1.3 mg/dm3). It has been established that the obtained mixed ligand systems are effective chelating agents and bind magnesium in an amount of 14 mg/cm3. The method of IR spectroscopy has proved that this system is formed with the participation of polydentant ligands. Determination of the pH stability of the complex showed that in the range of pH values 4–7, the chelate system is stable, at pH 2 only 10% of the complex is stored, at a pH of 9 – 60%. The thermostability of the complex was investigated by the method of differential scanning calorimetry. It was established that the complex is stable in the temperature range of 20-122 ° С, and therefore can be used as a physiologically functional ingredient in the health foods, the technology of which involves high-temperature processing.


2018 ◽  
Vol 85 (3) ◽  
pp. 339-346 ◽  
Author(s):  
Francisco Javier Espejo-Carpio ◽  
Raúl Pérez-Gálvez ◽  
Antonio Guadix ◽  
Emilia María Guadix

The enzymatic hydrolysis of milk proteins yield final products with improved properties and reduced allergenicity. The degree of hydrolysis (DH) influences both technological (e.g., solubility, water binding capacity) and biological (e.g., angiotensin-converting enzyme (ACE) inhibition, antioxidation) properties of the resulting hydrolysate. Phenomenological models are unable to reproduce the complexity of enzymatic reactions in dairy systems. However, empirical approaches offer high predictability and can be easily transposed to different substrates and enzymes. In this work, the DH of goat milk protein by subtilisin and trypsin was modelled by feedforward artificial neural networks (ANN). To this end, we produced a set of protein hydrolysates, employing various reaction temperatures and enzyme/substrate ratios, based on an experimental design. The time evolution of the DH was monitored and processed to generate the ANN models. Extensive hydrolysis is desirable because a high DH enhances some bioactivities in the final hydrolysate, such as antioxidant or antihypertensive. The optimization of both ANN models led to a maximal DH of 23·47% at 56·4 °C and enzyme–substrate ratio of 5% for subtilisin, while hydrolysis with trypsin reached a maximum of 21·3% at 35 °C and an enzyme–substrate ratio of 4%.


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