Studies on Immobilization of Penicillin G Acylase to Epoxy Resin

2012 ◽  
Vol 512-515 ◽  
pp. 1699-1711 ◽  
Author(s):  
Chao Fan ◽  
Ji Lie Li ◽  
Xiao Yuan Zhu ◽  
Nan Li ◽  
Wei Wang ◽  
...  
Keyword(s):  
Epoxy Resin ◽  
Immobilized Enzyme ◽  
Continuous Operation ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Process Conditions ◽  
Optimal Conditions ◽  
Optimum Temperature ◽  
Optimum Ph ◽  
Operation Stability

The process conditions of immobilizing penicillin G acylase(PGA) by epoxy resin were studied. This experiment used the Box-Behnken experimental design and response surface methodology(RSM) to optimize the conditions of immobilizing PGA by epoxy resin. The results showed the best process conditions were pH 8.1, temperature 29°C, carrier of epoxy resin 1g and reaction time 24 h. On these conditions, the activity of the immobilized enzyme was 365.76 U g-1, activity recovery rate was 62.82%. The characteristics of the immobilized PGA under optimal conditions had been measured and found that the optimum pH of immobilized enzyme was 9.0, the optimum temperature was 60°C. It has better continuous operation stability.

KINETIC STUDIES ON ACID PHOSPHATASE IN TRIBOLIUM CONFUSUM DUVAL

1964 ◽  
Vol 42 (12) ◽  
pp. 1769-1775 ◽  
Author(s):  
K. D. Chaudhary ◽  
S. Moorjani ◽  
A. Lemonde
Keyword(s):  
Kinetic Studies ◽  
Final Concentration ◽  
Tribolium Confusum ◽  
Metallic Ions ◽  
Optimal Conditions ◽  
Optimum Temperature ◽  
Apparent Effect ◽  
Michaelis Constant ◽  
Optimum Ph ◽  
Zero Order Reaction

The biochemical characteristics of acid phosphomonoesterase in Tribolium confusum homogenate have been determined. Zero-order reaction occurs for 30 minutes, with 10−3 M final concentration of phenyl phosphate at an optimum pH of 6.4. Michaelis constant (Km) under the optimal conditions is 6.34 × 10−3 M. Maximum enzyme activity is obtained at 40 °C, and the activation energy (ΔE) is 13,000 cal/mole, within the limits of optimum temperature. Inorganic phosphate inhibits competitively and Ki value is 3.45 × 10−3 M. Partial inhibition by fluoride is shown. Apparent effect of metallic ions also has been demonstrated.Comparison of these results with those reported in the literature for several other species of insects, as well as with those in certain mammalian systems, has been discussed.

Preparation of Genipin by Hydrolysis of Geniposide with Co-Immobilized Enzyme

2011 ◽  
Vol 236-238 ◽  
pp. 1793-1798 ◽  
Author(s):  
Hua Zheng Liang ◽  
He Chen ◽  
Jian Feng Wang ◽  
Yu Lan He
Keyword(s):  
High Performance ◽  
Immobilized Enzyme ◽  
Low Cost ◽  
Enzymatic Properties ◽  
High Yield ◽  
Cross Linking ◽  
Optimum Temperature ◽  
Environmental Friendly ◽  
Optimum Ph ◽  
Hydrolysis Of

Co-immobilize enzyme by cross-linking and embedding, optimize conditions for immobilizing, determinate the enzymatic properties of co-immobilized enzyme and study the methods for preparation of genipin using co-immobilized enzyme to hydrolyze geniposide. Optimized immobilizing conditions include glutaraldehyde concentration being 0.15%, cross-linking temperature being 20°C, cross-linking time being 2 hours, the activity of co-immobilized β-glucosidase and cell reaches to 65.33U/mg and the enzyme activity recovery being 52.63%. Enzymatic properties of co-immobilized enzyme are following: optimum temperature is 55°C and optimum pH is 5.0. The transformation experiments are carried out with co-immobilized enzyme. The results show that half-life of co-immobilized enzyme reaches around 40 days, higher than the normal immobilized enzyme. The conversion rate of geniposide is above 95% after 8 hours. The genipin is isolated, purified and recrystallized to reach more than 98% of purity by High Performance Liquid Chromatography. Advantages to prepare genipin using co-immobilized enzyme include low cost, high yield, environmental friendly and easy to manufacturing.

scholarly journals Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Catalysts ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 181 ◽  
Author(s):  
Wesam H. Abdulaal ◽  
Yaaser Q. Almulaiky ◽  
Reda M. El-Shishtawy
Keyword(s):  
Metal Ions ◽  
Immobilized Enzyme ◽  
Pmma Film ◽  
Optimum Temperature ◽  
Initial Activity ◽  
Casting Method ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Triton X ◽  
Enzyme Changes

Horseradish peroxidase (HRP) enzyme was effectively encapsulated onto an Fe3O4 nanoparticle–polymethyl methacrylate (PMMA) film via the casting method. The HRP was immobilized on the 0.5% Fe3O4Np–PMMA film and characterized by Fourier transform infrared spectroscopy and field emission scanning electron microscopy. Moreover, the reusability, thermal stability, optimum pH, optimum temperature, the influence of metal ions, and the effects of detergent and organic solvent were investigated. After optimizing the immobilization conditions, the highest efficiency of the immobilized enzyme was 88.4% using 0.5% Fe3O4Np–PMMA. The reusability of the immobilized HRP activity was 78.5% of its initial activity after being repeatedly used for 10 cycles. When comparing the free and immobilized forms of the HRP enzyme, changes in the optimum temperature and optimum pH from 30 to 40 °C and 7.0 to 7.5, respectively, were observed. The Km and Vmax for the immobilized HRP were estimated to be 41 mM, 0.89 U/mL for guaiacol and 5.84 mM, 0.66 U/mL for H2O2, respectively. The high stability of the immobilized HRP enzyme was obtained using metal ions, a high urea concentration, isopropanol, and Triton X-100. In conclusion, the applicability of immobilized HRP involves the removal of phenol in the presence of hydrogen peroxide, therefore, it could be a potential catalyst for the removal of wastewater aromatic pollutants.

scholarly journals Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae

2007 ◽  
Vol 72 (12) ◽  
pp. 1255-1263 ◽  
Author(s):  
Khaled Ahmed ◽  
Nenad Milosavic ◽  
Milica Popovic ◽  
Radivoje Prodanovic ◽  
Zorica Knezevic ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Thermal Stability ◽  
Immobilized Enzyme ◽  
Immobilized Enzymes ◽  
Optimum Temperature ◽  
Activity Profile ◽  
Original Activity ◽  
Yeast Saccharomyces Cerevisiae ◽  
Optimum Ph ◽  
Promising Solution

?-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of ?-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45 ?C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized ?-glucosidase.

Resolution of α/β-amino acids by enantioselective penicillin G acylase from Achromobacter sp .

2015 ◽  
Vol 122 ◽  
pp. 240-247 ◽  
Author(s):  
Michal Grulich ◽  
Jan Brezovský ◽  
Václav ŠtĿpánek ◽  
Andrea Palyzová ◽  
Eva Kyslíková ◽  
...  
Keyword(s):  
Amino Acids ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Achromobacter Sp

Immobilization and Characterization of Tannase and its Haze-removing

2009 ◽  
Vol 15 (6) ◽  
pp. 545-552 ◽  
Author(s):  
Erzheng Su ◽  
Tao Xia ◽  
Liping Gao ◽  
Qianying Dai ◽  
Zhengzhu Zhang
Keyword(s):  
Kinetic Parameter ◽  
High Activity ◽  
Green Tea ◽  
Storage Stability ◽  
Residual Activity ◽  
Black Tea ◽  
Optimum Temperature ◽  
Oolong Tea ◽  
Optimum Ph

Tannase was effectively immobilized on alginate by the method of crosslinking-entrapment-crosslinking with a high activity recovery of 76.6%. The properties of immobilized tannase were investigated. Its optimum temperature was determined to be 35 ° C, decreasing 10 °C compared with that of free enzyme, whereas the optimum pH of 5.0 did not change. The thermal and pH stabilities of immobilized tannase increased to some degree. The kinetic parameter, Km, for immobilized tannase was estimated to be 11.6 × 10-4 mol/L. Fe2+ and Mn2+ could activate the activity of immobilized tannase. The immobilized tannase was also applied to treat the tea beverage to investigate its haze-removing effect. The content of non-estern catechins in green tea, black tea and oolong tea increased by 52.17%, 12.94% and 8.83%, respectively. The content of estern catechins in green tea, oolong tea and black tea decreased by 20.0%, 16.68% and 5.04%, respectively. The anti-sediment effect of green tea infusion treated with immobilized tannase was significantly increased. The storage stability and reusability of the immobilized tannase were improved greatly, with 72.5% activity retention after stored for 42 days and 86.9% residual activity after repeatedly used for 30 times.

Porous thiiranyl polymers: Newer supports for immobilization of penicillin G acylase

1997 ◽  
Vol 33 (9) ◽  
pp. 1481-1485 ◽  
Author(s):  
S. Skaria ◽  
E.Sreenivasa Rao ◽  
S. Ponrathnam ◽  
K.K. Kumar ◽  
J.G. Shewale
Keyword(s):  
Penicillin G Acylase ◽  
Penicillin G
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