scholarly journals The inulin hydrolysis by recombinant exo-inulinases: determination the optimum temperatures and activation energies

2021 ◽  
Author(s):  
Justyna Miłek
Keyword(s):  
Activation Energies ◽  
Enzyme Concentration ◽  
Effect Of Temperature ◽  
High Yield ◽  
Production Environment ◽  
Recombinant Enzymes ◽  
Inulin Hydrolysis ◽  
Inulinase Activity ◽  
Hydrolysis Of ◽  
Deactivation Process

AbstractThe advantages of recombinant enzymes over native include the control in a production environment, product purity and also high yield. The paper presents the determination the optimum temperatures and the activation energies for various origin recombinant exo-inulinases, among others from Aspergillus niger, A. awamori, Kluyveromyces marxianus and K. cicerisporus. The parameters were estimated based on the literature of the activity curves versus temperature for hydrolysis of inulin. It was assumed that both the hydrolysis reaction process and the deactivation process of recombinant exo-inulinase were first-order reactions by the enzyme concentration. A mathematical model describing the effect of temperature on recombinant exo-inulinase activity was used. Based on the comparison analysis, values of the activation energies $${E_{\rm a }}$$ E a were in the range from $${32.01 \pm 7.80}$$ 32.01 ± 7.80 to $${43.83 \pm 4.87}$$ 43.83 ± 4.87 kJ mol$$^{-1}$$ - 1 , the deactivation energies $${E_{\rm d }}$$ E d were in the range from $${83.93 \pm 4.82}$$ 83.93 ± 4.82 to $${352.44 \pm 14.26}$$ 352.44 ± 14.26 kJ mol$$^{-1}$$ - 1 and the optimum temperature $${T_{\rm opt }}$$ T opt were obtained in the range from $${318.91 \pm }$$ 318.91 ± 1.19 to $${328.76 \pm 0.25}$$ 328.76 ± 0.25 K.

scholarly journals Determination of Activation Energies and the Optimum Temperatures of Hydrolysis of Starch by α-Amylase from Porcine Pancreas

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4117
Author(s):  
Justyna Miłek
Keyword(s):  
Pancreatic Insufficiency ◽  
Pharmaceutical Preparations ◽  
Activation Energies ◽  
Enzyme Concentration ◽  
Starch Hydrolysis ◽  
Effect Of Temperature ◽  
Porcine Pancreas ◽  
Hydrolysis Of ◽  
Deactivation Process

The present paper reports the determination of the activation energies and the optimum temperatures of starch hydrolysis by porcine pancreas α-amylase. The parameters were estimated based on the literature data on the activity curves versus temperature for starch hydrolysis by α-amylase from porcine pancreas. It was assumed that both the hydrolysis reaction process and the deactivation process of α-amylase were first-order reactions by the enzyme concentration. A mathematical model describing the effect of temperature on porcine pancreas α-amylase activity was used. The determine deactivation energies Ea were from 19.82 ± 7.22 kJ/mol to 128.80 ± 9.27 kJ/mol, the obtained optimum temperatures Topt were in the range from 311.06 ± 1.10 K to 326.52 ± 1.75 K. In turn, the values of deactivation energies Ed has been noted in the range from 123.57 ± 14.17 kJ/mol to 209.37 ± 5.17 kJ/mol. The present study is related to the starch hydrolysis by α-amylase. In the industry, the obtained results the values Ea, Ed, Topt can be used to design and optimize starch hydrolysis by α-amylase porcine pancreas. The obtained results might also find application in research on the pharmaceutical preparations used to treat pancreatic insufficiency or prognosis of pancreatic cancer.

Biological Conversion of Corncob Residues of Xylose Manufacture to L-Lactic Acid

2011 ◽  
Vol 236-238 ◽  
pp. 330-333 ◽  
Author(s):  
Tian Tian Sun ◽  
Ya Can Zhao ◽  
Jian Wu ◽  
Gui Fu Dai ◽  
Jun Ping Zhu
Keyword(s):  
Lactic Acid ◽  
Enzyme Concentration ◽  
High Yield ◽  
Sodium Acetate Buffer ◽  
Acid Fermentation ◽  
Reaction Conditions ◽  
Biological Conversion ◽  
Percent Conversion ◽  
Main Factors ◽  
Hydrolysis Of

The aim of this research is to study the saccharification of corncob residues of xylose manufacture by enzymes and turn it to L-lactic acid by fermentation. Corncob residues of xylose manufacture is one kind of lignocelluloses composed of 48.5% cellulose, 21.3% lignin, and 23.5% hemicellulose. As one of the most widely used organic acids in industry and the precursor of PLA, a degradable plastic, L-lactic acid is a very important material. In this study, six kinds of cellulases and one kind of β-glucosidase produced by different companies were studied to obtain high yield sugars needed for L-lactic acid fermentation. Results showed that composite of different enzymes could improve the catalysis effects. Mixture of cellulose F3: cellulose F4: β-glucosidase at the ratio of 2:4:9 engendered a high synergistic effect in hydrolysis. Also, the main factors influencing the hydrolysis of corncob residues were investigated. The appropriate reaction conditions are sodium acetate buffer 0.05-0.1mol/L, pH 5.0-5.5, concentration of corncob residues 15%, enzyme concentration 97U for 1g substrate, reaction temperature 50°C and the shaker speed 140 r/min. After 96h reaction, the concentration of glucose could reach as high as 5.5%. In fermentation, 4.48% of L-lactic acid was produced in 24 hours utilizing hydrolysis sugars as the carbon source, and the percent conversion of glucose to L- lactic acid was 81.5%.

Enzyme-assisted Extraction for Optimized Recovery of Phenolic Bioactives from Peganum hermala Leaves Using Response Surface Methodology

2018 ◽  
Vol 17 (4) ◽  
pp. 349-354
Author(s):  
Qadir Rahman ◽  
Anwar Farooq ◽  
Amjad Gilani Mazhar ◽  
Nadeem Yaqoob Muhammad ◽  
Ahmad Mukhtar
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Enzyme Concentration ◽  
Coumaric Acid ◽  
Assisted Extraction ◽  
Pre Treatment ◽  
Optimized Conditions ◽  
Enzyme Complexes ◽  
Hydrolysis Of ◽  
Central Composite

This study investigates the effect of enzyme formulations (Zympex-014, Kemzyme dry-plus and Natuzyme) on recovery of phenolics from Peganum hermala (harmal) leaves, under optimized conditions using response surface methodology. As compared to the other enzyme complexes, the yield (34 g/100g) obtained through Zympex-014-assisted extraction was higher under optimized conditions such as time (75 min), temperature (70°C), pH (6.5) and enzyme concentration (5 g/100 g) using central composite design (CCD). Effectiveness of Zympex-014 towards hydrolysis of P. hermala leaves cell wall was examined by analyzing the control and enzyme-treated leave residues using scanning electron microscope (SEM). GC/MS characterization authenticated the presence of quercetin (1.44), gallic acid (0.23), caffeic acid (0.04), cinnamic acid (0.05), m-coumaric acid (0.23) and p-coumaric acid (0.37 μg/g) as the potent phenolics in Zympex-014 based extract. It can be concluded from the findings of the current work that pre-treatment of P. hermala leaves with Zympex-014 significantly enhanced the recovery of phenolics that supports its potential uses in the nutra-pharamaceutical industry.

Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes

Microbiology ◽  
2004 ◽  
Vol 150 (7) ◽  
pp. 2257-2266 ◽  
Author(s):  
Helmuth Adelsberger ◽  
Christian Hertel ◽  
Erich Glawischnig ◽  
Vladimir V. Zverlov ◽  
Wolfgang H. Schwarz
Keyword(s):  
Extracellular Enzymes ◽  
Enzyme System ◽  
Thermophilic Bacterium ◽  
Recombinant Enzymes ◽  
Type Mode ◽  
Complete Set ◽  
First Time ◽  
Hydrolysis Of

Four extracellular enzymes of the thermophilic bacterium Clostridium stercorarium are involved in the depolymerization of de-esterified arabinoxylan: Xyn11A, Xyn10C, Bxl3B, and Arf51B. They were identified in a collection of eight clones producing enzymes hydrolysing xylan (xynA, xynB, xynC), β-xyloside (bxlA, bxlB, bglZ) and α-arabinofuranoside (arfA, arfB). The modular enzymes Xyn11A and Xyn10C represent the major xylanases in the culture supernatant of C. stercorarium. Both hydrolyse arabinoxylan in an endo-type mode, but differ in the pattern of the oligosaccharides produced. Of the glycosidases, Bxl3B degrades xylobiose and xylooligosaccharides to xylose, and Arf51B is able to release arabinose residues from de-esterified arabinoxylan and from the oligosaccharides generated. The other glycosidases either did not attack or only marginally attacked these oligosaccharides. Significantly more xylanase and xylosidase activity was produced during growth on xylose and xylan. This is believed to be the first time that, in a single thermophilic micro-organism, the complete set of enzymes (as well as the respective genes) to completely hydrolyse de-esterified arabinoxylan to its monomeric sugar constituents, xylose and arabinose, has been identified and the enzymes produced in vivo. The active enzyme system was reconstituted in vitro from recombinant enzymes.

Zur Chemie des Bis(methylsulfonyl)-amins (Dimesylamins), V [1] N-Chlorsulfonyl-methansulfonamid: Ein Produkt der Reaktion von Tetramethylsilan mit Imido-bis(schwefelsäurechlorid) / Investigations on Bis(methylsulphonyl)-amine (Dimesylamine), V [1] N-Chlorosulphonyl-methanesulphonamide: A Reaction Product from Tetramethylsilane and Imido-bis(sulphuryl chloride)

1983 ◽  
Vol 38 (6) ◽  
pp. 793-794 ◽  
Author(s):  
Armand Blaschette ◽  
Gerlinde Seurig
Keyword(s):  
High Yield ◽  
Reaction Conditions ◽  
Product Mixture ◽  
Moisture Sensitive ◽  
Hydrolysis Of ◽  
Complex Manner

AbstractTetramethylsilane reacts with HN(SO2Cl)2 (1) in a complex manner, the nature of the product mixture depending strongly on the reaction conditions. Refluxing 1 with TMS in excess, using CH2Cl2 as a diluent, affords in high yield the new compound HN(SO2Cl)(SO2Me) (2) according to eq. (3). Hydrolysis of the crystal-line, moisture sensitive compound 2 is described by eq. (4).

scholarly journals Production, characterization and application of inulinase from fungal endophyte CCMB 328

2012 ◽  
Vol 84 (2) ◽  
pp. 443-454 ◽  
Author(s):  
Diego S. Nascimento ◽  
Gildomar Valasques Junior ◽  
Pedro Fernandes ◽  
Geise C.A. Ribeiro ◽  
Danyo M. Lima ◽  
...  
Keyword(s):  
Response Surface Methodology ◽  
Yeast Extract ◽  
Arid Region ◽  
Culture Medium ◽  
Fungal Endophyte ◽  
Initial Concentration ◽  
Inulin Hydrolysis ◽  
Semi Arid Region ◽  
Hydrolysis Of ◽  
Semi Arid

Inulinase (β-2,1-D- fructan fructanohydrolase), EC 3.2.1.7, targets the β-2,1 linkage of inulin, a polyfructan consisting of linear β-2,1 linked fructose, and hydrolyzes it into fructose. This use provides an alternative to produce fructose syrup through the hydrolysis of inulin. The objective of this work was to study the production, characterization and applications of inulinases from the fungal endophyte CCMB 328 isolated from the Brazilian semi-arid region. Response Surface Methodology (RSM) was employed to evaluate the effect of variables (concentration of glucose and yeast extract), on secreted inulinase activities detected in the culture medium and also in the inulin hydrolysis. The results showed that the best conditions for inulinase production by CCMB 328 are 9.89 g / L for glucose and 1.09 g / L for yeast extract. The concentration of 0.20 mol/L of NaCl and KCl increased the activity of inulinase from CCMB 328 by approximately 63% and 37%, respectively. The results also showed that the inulinase has potential for inulin hydrolysis, whose conversion yields roughly 72.48 % for an initial concentration of inulin at 1% (w/v).

scholarly journals Kinetics of Enzymatic Hydrolysis of Southeast Sulawesi Sago Starch

2020 ◽  
pp. 53-61
Author(s):  
Ansharullah Ansharullah ◽  
Muhammad Natsir
Keyword(s):  
Enzymatic Hydrolysis ◽  
Maximum Velocity ◽  
Enzyme Concentration ◽  
Hydrolysis Rate ◽  
Sago Starch ◽  
Optimum Conditions ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Substrate Concentrations ◽  
Menten Constant

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.

scholarly journals Isolation of Free Amino Acids via Enzymatic Hydrolysis of Tobacco-Derived F1 Protein

2018 ◽  
Vol 28 (4) ◽  
pp. 179-190
Author(s):  
Mehdi Ashraf-Khorassani ◽  
William M. Coleman ◽  
Michael F. Dube ◽  
Larry T. Taylor
Keyword(s):  
Amino Acids ◽  
Enzymatic Hydrolysis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Concentration ◽  
Enzyme Concentration ◽  
Enzymatic Conversion ◽  
Reaction Conditions ◽  
Analytical Methodology ◽  
Hydrolysis Of

SummaryFree amino acids have been isolated via optimized enzymatic hydrolysis of F1 tobacco protein using two cationic resins (Amberlite IR120 and Dowex MAC-2). Optimized enzymatic conversions of the protein as a result of systematic variations in conditions (e.g., time, temperature, pH, enzyme type, enzyme concentration, anaerobic/aerobic environments, and protein concentration) employing commercially available enzymes, were consistently higher than 50% with qualitative amino acid arrays that were consistent with the known composition of tobacco F1 protein. Amberlite IR120 was shown to have a much higher efficiency and capacity for isolation of amino acids from standard solutions and from hydrolysate when compared with the results using Dowex MAC-2. Two columns packed with conditioned Amberlite IR120 (120 × 10 mm,12–15 g resin) and (200 × 25.4 mm, 60–65 g resin) were used to isolate two batches (2.5–3.0 mg and 13–15 mg) of free amino acids, respectively. A relatively inexpensive analytical methodology was developed for rapid analysis of the free amino acids contained within the enzyme hydrolysate. Commercially available enzymes, when employed in optimized reaction conditions, are very effective for enzymatic conversion of tobacco F1 protein to free amino acids.

scholarly journals Enzymatic hydrolysis of oil palm empty fruit bunch to produce reducing sugar and its kinetic Hidrolisis enzimatik tandan kosong kelapa sawit untuk menghasilkan gula pereduksi dan kinetikanya

2016 ◽  
Vol 83 (1) ◽  
Author(s):  
Vera BARLIANTI ◽  
Deliana DAHNUM ◽  
. MURYANTO ◽  
Eka TRIWAHYUNI ◽  
Yosi ARISTIAWAN ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Oil Palm ◽  
Volume Ratio ◽  
Enzyme Concentration ◽  
Reducing Sugar ◽  
Economic Feasibility ◽  
First Order ◽  
Empty Fruit Bunches ◽  
Hydrolysis Process ◽  
Hydrolysis Of

Abstrak Sebagai salah satu Negara penghasil minyak kelapa sawit mentah (CPO), Indonesia juga menghasilkan tandan kosong kelapa sawit (TKKS) dalam jumlah besar. TKKS terdiri dari-tiga-komponen utama, yaitu selulosa, hemiselulosa, dan lignin. Pengolahan awal TKKS secara alkalindi ikuti dengan hidrolisis TKKS secara enzimatik menggunakan kombinasi enzim selulase dan β-glukosidase akan menghasilkan gula-gula yang mudah difermentasi.  Penelitian ini bertujuan untuk mempelajari pengaruh konsentrasi substrat, kon-sentrasi enzim, dan suhu selama proses hidrolisis berlangsung.  Hasil yang diperoleh menunjukkan bahwa konsentrasi gula maksimum (194,78 g/L) dicapai pada konsentrasi TKKS 20% (b/v), konsentrasi campuran enzim yang terdiri dari selulase dan β-1,4 glukosidase sebesar 3,85% (v/v), dan suhu 50oC. Perbandingan antara selulase dan β-1,4 glukosidase adalah 5:1 dengan masing-masing aktivitas enzim sebesar 144.5 FPU/mL dan 63 FPU/mL. Hasil penelitian juga menunjukkan bahwa model kinetika yang sesuai untuk proses hidrolisis TKKS secara enzimatik adalah model kinetika Shen dan Agblevor dengan reakside aktivasi enzim orde satu.  Hasil ini mendukung studi kelayakan ekonomi dalam pemanfaatan TKKS untuk produksi bioetanol.AbstractAs one of the crude palm oil producers, Indonesia also produces empty fruit bunches (EFB)in large quantities. The oil palm EFB consist of cellulose, hemicellulose and lignin. Alkaline pretreatment of EFB, followed by enzymatic hydro-lysis of cellulose using combination of cellulase and β-glucosidase enzymes produce fermentable sugars. This paper reported the effects of substrate loading, enzyme concentration, and temperature of hydrolysis process on reducing sugar production. The  maximum  sugar  concentration (194.78 g/L) was produced at 50oC using 20% (w/v) EFB and 3.85% (v/v) mixed enzymes of cellulase and β-1,4 glucosidase in volume ratio of 5:1 (v/v), with enzyme activity of 144.5 FPU/mL and 63 FPU/mL, respectively. The results also showed that the suitable kinetic model for enzymatic hydrolysis process of oil palm EFB follow Shen and Agblevor model with first order of enzyme deactivation. These results support the economic feasibility study in utilization of EFB of oil palm for bioethanol production.    

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