scholarly journals Immobilization of invertase and glucoamylase on a macroporous copolymer of etyleneglycoldimethacrylate and glycidyl methacrylate and potential applications in biotechnology

2003 ◽  
Vol 57 (11) ◽  
pp. 536-542 ◽  
Author(s):  
Radivoje Prodanovic ◽  
Nenad Milosavic ◽  
Slobodan Jovanovic ◽  
Zoran Vujcic

The optimal conditions for the immobilization of invertase and glucoamylasewere found via their carbohydrate moiety on a macroporous copolymer of ehtyleneglycoldimethacry late and glycidylmethacrylate. Almost all of the added enzyme was bound to the polymer by increasing the time of incubation of the oxidized enzyme with polymer. A specific activity of 5500 U/g for invertase was obtained and 1100 U/g for glucoamylase. The specific productivity for invertase in a packed bed reactor was 3.5 kg/lh and for glucoamylase 1.9 kg/lh. During continuous use in a packed bed the reactor operational half life for invertase was 290 days, while no decrease in activity was observed for glucoamylase. In 50% (v/v) ethanol the immobilized enzymes were five to ten times more stable, and more than 200 times more stable in 25% (v/v) dioxane. The immobilized enzymes retained all activity in petroleum ether after 3 days of incubation. Because of their higher stability over native enzymes, and the large surface area of the polymer immobilized glucoamylase and invertase could be more useful for glycoside synthesis in non-aqueous solvents than native ones.

Biomolecules ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 646 ◽  
Author(s):  
Jakub Zdarta ◽  
Tomasz Machałowski ◽  
Oliwia Degórska ◽  
Karolina Bachosz ◽  
Andriy Fursov ◽  
...  

For the first time, 3D chitin scaffolds from the marine demosponge Aplysina archeri were used for adsorption and immobilization of laccase from Trametes versicolor. The resulting chitin–enzyme biocatalytic systems were applied in the removal of tetracycline. Effective enzyme immobilization was confirmed by scanning electron microscopy. Immobilization yield and kinetic parameters were investigated in detail, in addition to the activity of the enzyme after immobilization. The designed systems were further used for the removal of tetracycline under various process conditions. Optimum process conditions, enabling total removal of tetracycline from solutions at concentrations up to 1 mg/L, were found to be pH 5, temperature between 25 and 35 °C, and 1 h process duration. Due to the protective effect of the chitinous scaffolds and stabilization of the enzyme by multipoint attachment, the storage stability and thermal stability of the immobilized biomolecules were significantly improved as compared to the free enzyme. The produced biocatalytic systems also exhibited good reusability, as after 10 repeated uses they removed over 90% of tetracycline from solution. Finally, the immobilized laccase was used in a packed bed reactor for continuous removal of tetracycline, and enabled the removal of over 80% of the antibiotic after 24 h of continuous use.


Author(s):  
Mi Na Choi ◽  
Kyung-Chul Shin ◽  
Dae Wook Kim ◽  
Baek-Joong Kim ◽  
Chang-Su Park ◽  
...  

Rare sugars are regarded as functional biological materials due to their potential applications as low-calorie sweeteners, antioxidants, nucleoside analogs, and immunosuppressants. D-Allose is a rare sugar that has attracted substantial attention in recent years, owing to its pharmaceutical activities, but it is still not widely available. To address this limitation, we continuously produced D-allose from D-allulose using a packed bed reactor with commercial glucose isomerase (Sweetzyme IT). The optimal conditions for D-allose production were determined to be pH 8.0 and 60°C, with 500 g/L D-allulose as a substrate at a dilution rate of 0.24/h. Using these optimum conditions, the commercial glucose isomerase produced an average of 150 g/L D-allose over 20 days, with a productivity of 36 g/L/h and a conversion yield of 30%. This is the first report of the successful continuous production of D-allose from D-allulose by commercial glucose isomerase using a packed bed reactor, which can potentially provide a continuous production system for industrial applications of D-allose.


2003 ◽  
Vol 68 (11) ◽  
pp. 819-824 ◽  
Author(s):  
Radivoje Prodanovic ◽  
Milos Simic ◽  
Zoran Vujcic

Periodate oxidized invertase was immobilized by adsorption on sepiolite. The obtained immobilized enzyme was more resistant to washing out by concentrated salt solution, and had an eight times higher half-life at 60 ?C than adsorbed native invertase. In packed bed reactor 50 % conversion of 500 g/dm3 sucrose at 40 ?C and a flow rate of 1 bv/h was achieved. The specific productivity of the immobilized invertase was O.187 kg/dm3/h.


2021 ◽  
Vol 407 ◽  
pp. 127065
Author(s):  
Robert D. Franklin ◽  
Joshua A. Whitley ◽  
Adam A. Caparco ◽  
Bettina R. Bommarius ◽  
Julie A. Champion ◽  
...  

2017 ◽  
Vol 224 ◽  
pp. 292-297 ◽  
Author(s):  
Juntao Xu ◽  
Changsheng Liu ◽  
Meng Wang ◽  
Lei Shao ◽  
Li Deng ◽  
...  

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