scholarly journals Kinetic Modeling of the Formation of Peptide Nanoparticles by Tryptic Hydrolysis of Β-Casein

INEOS OPEN ◽  
2021 ◽  
Author(s):  
A. V. Golovanov ◽  
◽  
M. M. Vorob'ev ◽  

Peptide nanoparticles obtained by the enzymatic hydrolysis of proteins are new biocompatible nontoxic systems for the transport of biologically active compounds. The formation of peptide nanoparticles from -casein during its controlled hydrolysis by trypsin was modeled by the methods of chemical kinetics. The product of the time of nanoparticle formation (tmax) by the enzyme concentration (E0) was analyzed in different kinetic models. The dependence of tmax∙E0 on the enzyme concentration was used to estimate the contribution of the enzymatic and non-enzymatic stages to the formation of nanoparticles.

Revista Vitae ◽  
2018 ◽  
Vol 25 (1) ◽  
pp. 17-25
Author(s):  
José Edgar ZAPATA MONTOYA ◽  
◽  
Diego Enrique GIRALDO-RIOS ◽  
Andrea Johana BAÉZ-SUAREZ ◽  
◽  
...  

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.


Author(s):  
Mehdi Ashraf-Khorassani ◽  
William M. Coleman ◽  
Michael F. Dube ◽  
Larry T. Taylor

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.


2016 ◽  
Vol 83 (1) ◽  
Author(s):  
Vera BARLIANTI ◽  
Deliana DAHNUM ◽  
. MURYANTO ◽  
Eka TRIWAHYUNI ◽  
Yosi ARISTIAWAN ◽  
...  

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.    


2015 ◽  
Vol 104 ◽  
pp. 10-19 ◽  
Author(s):  
J.D. Angarita ◽  
R.B.A. Souza ◽  
A.J.G. Cruz ◽  
E.C. Biscaia ◽  
A.R. Secchi

2009 ◽  
Author(s):  
Yi Zheng ◽  
Zhongli Pan ◽  
Ruihong Zhang ◽  
Bryan M Jenkins

2018 ◽  
Vol 12 (2) ◽  
Author(s):  
A. Kapustian ◽  
N. Cherno ◽  
О. Nikulina

The possibility of obtaining bioavailable mixed ligand chelate complexes of calcium has been considered. As bioligands, it is proposed to use the metabolic products of probiotic bacteria combination and products of enzymatic hydrolysis of peptidoglycans of their cell walls. The culture fluid of probiotic bacteria composition has been investigated for the determination of metabolites in its composition that can participate in the formation of calcium chelate complexes. The qualitative composition and quantitative content of organic acids of a culture fluid have been determined. It has been established that it contains the following acids: oxalic (1.6 mg/dm3), citric (22.1 mg/dm3), acetic (575.8 mg/dm3), lactic (236.3 mg/dm3), benzoic (1.5 mg/dm3). In addition, it has been found that in the composition of the culture liquid, free amino acids and soluble protein are also present in the amount of 1.2 mg/cm3 and 5 mg/cm3, respectively.In order to obtain fragments of peptidoglycans of cell walls of probiotic bacteria as potential bioligands for complex formation, their enzymatic hydrolysis with pancreatin has been performed. It has been established that the highest content of biologically active muropeptides is 5.1 mg/cm3 and it is accumulated during hydrolysis of the substrate for 180 minutes, the ratio of enzyme: substrate 1: 100 and 5.1 mg/cm3.By methods of nephelometry and spectrophotometry, it has been established that the obtained mixed ligand systems are effective chelating agents and, depending on the composition, bind calcium in amounts of 9, 14 and 16 mg/cm3. Identification of the pH stability of the complex has been shown 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 pH 9 60% is preserved. By method of differential scanning calorimetry the thermostability of the complex has been investigated. It has been established that the complex is stable in the temperature range of 20–122°С, and therefore can be used in the composition of health foods, the technology of which involves high-temperature processing.


2020 ◽  
Vol 3 (2) ◽  
pp. 98-107
Author(s):  
Galileo E. Araguirang ◽  
Arianne Joyce R. Arizala ◽  
Eden Beth B. Asilo ◽  
Jamie Louise S. Batalon ◽  
Erin B. Bello ◽  
...  

Banana (M. acuminata x balbisiana) is an abundant lignocellulosic waste material in large plantations all over the Philippines, especially in Mindanao, which can be utilized as substrate in producing high-value products like ethanol. To compensate for the low yield based on total weight of substrate due to the high moisture content of banana pseudostem, there is the primary challenge to make the conversion of this lignocellulosic biomass into monomeric sugar and then into ethanol more efficiently in order to achieve yields that would make it cost-competitive. Hence, this study evaluated the effects of solid loading, incubation time and amount of enzyme on yield of reducing sugars in the enzymatic hydrolysis process and attempted to optimize the significant factors by Response Surface Methodology (RSM), specifically using Box-Behnken design. There was significant improvement on the reducing sugar yield of the pretreated banana pseudostem at 20 h incubation time, 15 g solid loading and 0.55 % enzyme concentration. Ethanol production was observed to be higher in the detoxified substrate although biomass was higher for the non-detoxified substrate. As to our knowledge, the present study is the first attempt to produce second generation ethanol using banana pseudostem waste as feedstock in the Philippines.


1985 ◽  
Vol 27 (9) ◽  
pp. 1282-1290 ◽  
Author(s):  
G. Caminal ◽  
J. López-Santín ◽  
C. Solà

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