Enzymatic activities of proteases immobilized on tri(4-formyl phenoxy) cyanurate

Rao, R. Srinivasa; Borkar, Prita S.; Khobragade, Chandrahasya N.; Sagar, A. D.

doi:10.1016/j.enzmictec.2006.03.020

Cited by 28 publications

(3 citation statements)

References 31 publications

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“…The above results are supported by Srinivasa Rao et al [28], who emphasized that immobilization of α -chymotrypsin, trypsin, and pepsin on tri(4-formyl phenoxy) cyanurate revealed a shift in optimum temperature from 40 to 50°C for α -chymotrypsin and trypsin and 50 to 60°C for papain. Amaral et al [29], on the other hand, reported that fish trypsin immobilized on ferromagnetic dacron had an optimum temperature of 50°C which was lower than that found for the soluble enzyme at 55°C.…”

Section: Resultssupporting

confidence: 62%

Optimization and Immobilization of Purified Labeo rohita Visceral Protease by Entrapment Method

Geethanjali

Subash

2013

Enzyme Research

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The purified fish visceral protease enzyme was immobilized by using various concentrations of sodium alginate and calcium chloride to optimize the best concentration for the formation of the beads. Then it was characterized by assaying the optimal pH, temperature, storage stability and reusability. The results on immobilization with sodium alginate and calcium chloride showed that a combination of 2% sodium alginate and 0.3 M calcium chloride weas found to be the optimum concentration for the formation of spherical and stable beads, this gave a maximal entrapped activity of 48.31%, and there was no change in the optimum pH 8.0 and temperature 40°C of protease before and after entrapment. The results on stability and reusability indicated that it was stable at 4°C retaining 100% residual activity after 5 days of storage and 67% loss of activity after ten days of storage and it retained 100% residual activity on the first reuse, 75% residual activity on the second reuse, 25% residual activity on the third use and complete loss in the activity on the fourth reuse.

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Section: Resultssupporting

confidence: 62%

Optimization and Immobilization of Purified Labeo rohita Visceral Protease by Entrapment Method

Geethanjali

Subash

2013

Enzyme Research

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“…As shown in Figure , an optimum enzyme activity was observed at pH 6.8 for free urease and pH 7.2 for tethered urease. Similar results have been previously reported in refs and . The alkaline shift of maximum activity could be due to a higher H + concentration in the microenvironment of the support because lots of acidic groups were generated due to HNO 3 oxidation.…”

Section: Resultssupporting

confidence: 90%

Development of Coconut Shell Activated Carbon-Tethered Urease for Degradation of Urea in a Packed Bed

Wang

Deng

et al. 2013

ACS Sustainable Chem. Eng.

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Coconut shell activated carbon (AC)-tethered urease (from jack bean) was successfully developed to degrade urea in a packed bed reactor. The loading capacity of urease in AC was 78.8 mg/g. The tethered enzyme showed a maximum activity at 70 °C and pH 7.2. For higher than 75% of the maximum activity, the tethered urease showed a broader temperature range of 42–80 °C compared to 45–75 °C for the free enzyme. Similarly, the tethered urease had an increased stability against the changes of pH. The K m value of the free urease was 0.271 mol/L and 0.345 mol/L for the tethered one. This may be caused by the conformational changes of the enzyme. The V max values were 0.215 and 0.110 mol/min for the tethered and free ureases, respectively, which is reflected by an increase in catalytic activity. The catalytic degradation of urea was performed in a packed bed reactor. The remaining activity of the tethered urease was over 80% after 50 h of operation.

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“…The reaction was continued further at the same temperature for 3 h. At the end of the reaction, the solution in the flask was poured on the crushed ice. The white product so formed was separated by filtering through Whatman paper No I and washed several times with distilled water and dried under reduced pressure at 100 o C for 5-6 h [25]. The synthesized product tri (4-formyl phenoxy) cyanurate was designated as A and was monitored by thin layer chromatography [26].…”

Section: Synthesis and Characterization Of Tri (4-formyl Phenoxy) Cyamentioning

confidence: 99%

Immobilization and stabilization of Pseudomonas aeruginosa SRT9 lipase on tri(4-formyl phenoxy) cyanurate

Prita

Chandrahas

Ramana

et al. 2011

Korean J. Chem. Eng.

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Lipase was extracted and purified from Pseudomonas aeruginosa SRT9. Culture conditions were optimized and highest lipase production amounting to 147.36 U/ml was obtained after 20 h incubation. The extracellular lipase was purified on Mono QHR5/5 column, resulting in a purification factor of 98-fold with specific activity of 12307.81 U/mg. Lipase was immobilized on tri (4-formyl phenoxy) cyanurate to form Schiff's base. An immobilization yield of 85% was obtained. The native and immobilized lipases were used for catalyzing the hydrolysis of olive oil in aqueous medium. Comparative study revealed that immobilized lipase exhibited a shift in optimal pH from 6.9 (free lipase) to 7.5 and shift in optimal temperature from 55 o C to 70 o C. The immobilized lipase showed 20-25% increase in thermal stability and retained 75% of its initial activity after 7 cycles. It showed good stability in organic solvents especially in 30% acetone and methanol. Enzyme activity was decreased by ~60% when incubated with 30% butanol. The kinetic studies revealed increase in K M value from 0.043 mM (native) to 0.10 mM for immobilized lipase. It showed decrease in the V max of immobilized enzyme (142.8 µmol min −1 mg −1 ), suggesting enzyme activity decrease in the course of covalent binding. The immobilized lipase retained its initial activity for more than 30 days when stored at 4 o C in TrisHCl buffer pH 7.0 without any significant loss in enzyme activity.

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Enzymatic activities of proteases immobilized on tri(4-formyl phenoxy) cyanurate

Cited by 28 publications

References 31 publications

Optimization and Immobilization of Purified Labeo rohita Visceral Protease by Entrapment Method

Optimization and Immobilization of Purified Labeo rohita Visceral Protease by Entrapment Method

Development of Coconut Shell Activated Carbon-Tethered Urease for Degradation of Urea in a Packed Bed

Immobilization and stabilization of Pseudomonas aeruginosa SRT9 lipase on tri(4-formyl phenoxy) cyanurate

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