Kinetics of Enzymatic Hydrolysis of Southeast Sulawesi Sago Starch

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.

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THE KINETICS OF TRYPSIN DIGESTION

The Journal of General Physiology ◽

10.1085/jgp.6.4.439 ◽

1924 ◽

Vol 6 (4) ◽

pp. 439-452

Author(s):

John H. Northrop

Keyword(s):

Enzyme Concentration ◽

Experimental Results ◽

Trypsin Digestion ◽

First Approximation ◽

High Enzyme ◽

Rate Of Hydrolysis ◽

High Concentrations ◽

Kinetics Of ◽

Hydrolysis Of ◽

Substrate Concentrations

The rate of hydrolysis of edestin by trypsin at 40° and in the presence of 1 M NaCl has been studied. Under these conditions the enzyme is rapidly inactivated and the equation for the reaction may be written See PDF for Equation in which Et is the concentration of enzyme during the interval (T1–T2). This equation has been tested by determining the enzyme concentration at various times during the reaction and substituting these values in the above equation. The experimental results agree with this formula when the initial enzyme or edestin concentrations are varied. No anomalous results of varying substrate concentrations are apparent. It can further be assumed as a first approximation that the enzyme is decomposing monomolecularly and the equation can then be written See PDF for Equation This equation is also satisfactory provided high enzyme concentrations and low edestin concentrations are used. With high concentrations of edestin and low trypsin the effects of the products of the reaction on the enzyme become too large to be neglected and the formula no longer holds.

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Study on the Kinetics of Salmon Skin Proteolysis

Nanoscience and Nanotechnology Letters ◽

10.1166/nnl.2019.3054 ◽

2019 ◽

Vol 11 (12) ◽

pp. 1706-1710

Author(s):

Yiping Xia ◽

Hao Yu ◽

Yaoguang Zhong

Keyword(s):

Enzymatic Hydrolysis ◽

Kinetic Model ◽

Kinetic Mechanism ◽

Reaction Rate Constant ◽

Hydrolysis Rate ◽

Degree Of Hydrolysis ◽

Hydrolysis Process ◽

Skin Protein ◽

Kinetics Of ◽

Hydrolysis Of

In this study, in order to study the kinetic mechanism of enzymatic hydrolysis of salmon protein, the kinetic model of enzymatic hydrolysis of salmon skin protein by papain was established. The skin protein of salmon was hydrolyzed by papain under the following conditions: the mass concentration of salmon skin protein is 55 g/L, the initial papain concentration is 2.0 g/L, the pH of enzymatic solution is 7.2 and the temperature of enzymatic hydrolysis is 55 °C. Finally, the kinetic model of hydrolysis was established as follows: Hydrolysis rate R =(27.217E0–0 0357S0exp[–0.2587(DH)]; Degree of hydrolysis DH = 3.879 ln[1 + 7.0165E0/S0 –0.0092t]. The reaction rate constant k3 = 27.217 min–1 and the enzyme deactivation constant kd = 7.0752 min–1 were deduced to control the enzymatic hydrolysis process. Further verification tests showed that the theoretical value of the degree of hydrolysis of the model was basically consistent with the actual value, and the kinetic model had certain practical value, indicating that the established salmon skin protease kinetic model could be used to guide and optimize the enzymatic hydrolysis process.

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Activity of some enzymes, participating in nitrogen compounds transformation in chernozem, polluted by fluorine compounds

Acta Agraria Debreceniensis ◽

10.34101/actaagrar/38/2767 ◽

2010 ◽

pp. 99-104

Author(s):

Vitalii Gryshko

Keyword(s):

Enzymatic Hydrolysis ◽

Enzymatic Reaction ◽

Nitrogen Compounds ◽

Maximal Velocity ◽

Correlation Dependence ◽

Fluorine Compounds ◽

Physical And Chemical ◽

Kinetics Of ◽

Hydrolysis Of ◽

Menten Constant

Contamination of chernozem by fluorine compounds variously affects those enzymes (urease, asparaginase, glutaminase, arginase, amidase), which takes part in the metabolism of nitrogen-bearing organic compounds. In broken soils the inhibited desaminisations is stronger, than enzymatic hydrolysis of asparagine and arginine. The features of seasonal dynamics of change activity of urease and correlation dependence of its activity from some physical and chemical soils properties are described. These tendencies well comport with the results of model experiments. At minimum HF influence there is inhibition of processes of monohydrocarboxylic acids desaminisation, hydrolytic breaking up of arginine and glutamine. By a side with this there is activating of urea and asparagine breaking up processes on the initial stages of toxicant influence. The study of kinetics of process of urea enzymatic hydrolysis in chernozem at the different level of HF influence showed changes of initial and maximal velocity of enzymatic reaction, and also Michaelis-Menten constant.

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Effect of Particle Size on the Kinetics of Enzymatic Hydrolysis of Microcrystalline Cotton Cellulose: a Modeling and Simulation Study

Applied Biochemistry and Biotechnology ◽

10.1007/s12010-018-2856-6 ◽

2018 ◽

Vol 187 (3) ◽

pp. 800-816 ◽

Cited By ~ 1

Author(s):

Ashwin Gaikwad

Keyword(s):

Particle Size ◽

Enzymatic Hydrolysis ◽

Modeling And Simulation ◽

Simulation Study ◽

Cotton Cellulose ◽

Effect Of Particle Size ◽

Kinetics Of ◽

Hydrolysis Of

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Kinetics of enzymatic hydrolysis of rice straw by the pretreatment with a bio-based basic ionic liquid under ultrasound

Process Biochemistry ◽

10.1016/j.procbio.2015.01.013 ◽

2015 ◽

Vol 50 (4) ◽

pp. 623-629 ◽

Cited By ~ 15

Author(s):

Chun-Yao Yang ◽

Tony J. Fang

Keyword(s):

Ionic Liquid ◽

Enzymatic Hydrolysis ◽

Rice Straw ◽

Basic Ionic Liquid ◽

Kinetics Of ◽

Hydrolysis Of

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Enzymatic hydrolysis of sago starch

Food Chemistry ◽

10.1016/0308-8146(94)90014-0 ◽

1994 ◽

Vol 49 (4) ◽

pp. 411-417 ◽

Cited By ~ 7

Author(s):

S. Gorinstein ◽

C.G. Oates ◽

Sh.-M. Chang ◽

Ch.-Yi. Lii

Keyword(s):

Enzymatic Hydrolysis ◽

Sago Starch ◽

Hydrolysis Of

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

Beiträge zur Tabakforschung International/Contributions to Tobacco Research ◽

10.2478/cttr-2018-0017 ◽

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.

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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

E-Journal Menara Perkebunan ◽

10.22302/ppbbi.jur.mp.v83i1.12 ◽

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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Kinetics of alkoxysilanes hydrolysis: An empirical approach

Scientific Reports ◽

10.1038/s41598-019-54095-0 ◽

2019 ◽

Vol 9 (1) ◽

Cited By ~ 1

Author(s):

Ahmed A. Issa ◽

Marwa El-Azazy ◽

Adriaan S. Luyt

Keyword(s):

Reaction Mechanisms ◽

Hydrolysis Reaction ◽

Hydrolysis Rate ◽

Coupling Agents ◽

Linear Free Energy Relationship ◽

Acidic Media ◽

Linear Free Energy ◽

Primary Materials ◽

Kinetics Of ◽

Hydrolysis Of

AbstractAlkoxysilanes and organoalkoxysilanes are primary materials in several industries, e.g. coating, anti-corrosion treatment, fabrication of stationary phase for chromatography, and coupling agents. The hydrolytic polycondensation reactions and final product can be controlled by adjusting the hydrolysis reaction, which was investigated under a variety of conditions, such as different alkoxysilanes, solvents, and catalysts by using gas chromatography. The hydrolysis rate of alkoxysilanes shows a dependence on the alkoxysilane structure (especially the organic attachments), solvent properties, and the catalyst dissociation constant and solubility. Some of the alkoxysilanes exhibit intramolecular catalysis. Hydrogen bonding plays an important role in the enhancement of the hydrolysis reaction, as well as the dipole moment of the alkoxysilanes, especially in acetonitrile. There is a relationship between the experimentally calculated polarity by the Taft equation and the reactivity, but it shows different responses depending on the solvent. It was found that negative and positive charges are respectively accumulated in the transition state in alkaline and acidic media. The reaction mechanisms are somewhat different from those previously suggested. Finally, it was found that enthalpy–entropy compensation (EEC) effect and isokinetic relationships (IKR) are exhibited during the hydrolysis of CTES in different solvents and catalysts; therefore, the reaction has a linear free energy relationship (LFER).

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