Nuclease p1 immobilized on deae cellulose

Shi, Lu-E; Yi, Yu; Tang, Zhen‐Xing; Xiong, Wen-Yue; Mei, Jiang-Feng

doi:10.1590/s0104-66322010000100003

Cited by 12 publications

(11 citation statements)

References 21 publications

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“…The current results are similar to the immobilization of nuclease p1 on DEAE-cellulose (Shi et al, 2010). DEAE-cellulose can absorb a lot of spores in a short time, but the spore distribution on the fiber surface is not uniform (Figure 2).…”

Section: Discussionsupporting

confidence: 79%

PREPARATION AND CHARACTERIZATION OF IMMOBILIZED SPORES WITH LACCASE ACTIVITY FROM Bacillus pumilus W3 ON DEAE-CELLULOSE AND THEIR APPLICATION IN DYE DECOLORIZATION

Zhou

Zhang

Cai

et al. 2017

Braz. J. Chem. Eng.

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-In order to obtain a more stable and reusable immobilized spore laccase for dye decolorization, the spores from Bacillus pumilus W3 were immobilized on diethylaminoethyl cellulose (DEAE-cellulose). Free and immobilized spore laccase retained 34.38% and 46.11% of their initial activity, respectively, after 10 days incubation at pH 9.0. Their residual activity remained at 27.36% and 31.84% after 10 h incubation at 70 °C. Immobilized spore laccase was more stable than free spore laccase in the presence of most organic solvents, metal ions and inhibitors. The tested dyes, including methyl green, methyl red and acid red 1, were removed 86.82%, 78.14% and 88.60%, respectively, by immobilized spore laccase after 24 h at 37 °C, and 74.34% of initial decolorization activity after 7 cycles was retained when it decolorized acid red 1. These properties indicated that immobilized spore laccase may be useful in textile effluent treatment.

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Section: Discussionsupporting

confidence: 79%

PREPARATION AND CHARACTERIZATION OF IMMOBILIZED SPORES WITH LACCASE ACTIVITY FROM Bacillus pumilus W3 ON DEAE-CELLULOSE AND THEIR APPLICATION IN DYE DECOLORIZATION

Zhou

Zhang

Cai

et al. 2017

Braz. J. Chem. Eng.

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“…The biotransformation of natural products is usually conducted under mild conditions, rather than at an improper pH, high salt concentration, high substrate concentration, and high temperature. Thus, the use of immobilized enzymes in transformation of natural products effectively avoids detachment from the DEAE-52 cellulose carrier due to such improper reaction conditions (Bai et al, 2005;Karboune et al, 2005;Shi et al, 2010;Ashraf et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

“…However, the immobilized enzyme retained its higher activity at pH≥6.5 while free enzyme retained its higher activity at pH≤6.5. These small changes of enzymic activity with pH may be attributed to the effect of the negativelycharged support for enzyme immobilization which will result in a basic shift in the pH optimum (Goldstein et al, 1964;Shi et al, 2010). …”

Section: Optimal Ph For Immobilized Enzymementioning

confidence: 99%

“…The value of Km for immobilized enzyme was approximately 6.4 times higher than that of the free enzyme. This increase may reflect the reduction of the affinity of the substrate for the active site of the enzyme which resulted from conformational and steric modifications of the enzyme introduced by binding to DEAE-52 cellulose and the substrate transfer resistance inherent in the morphology of the support (Shi et al, 2010). …”

Section: Kinetic Constant Kmmentioning

confidence: 99%

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Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Liu

Sun

et al. 2014

Braz. J. Chem. Eng.

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-For immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 on DEAE-52 cellulose, the optimal amount of enzyme protein was 12 mg protein: 1 g DEAE-52 cellulose; the optimal pH was 6.5; and the optimal immobilization time was 6 hr. The specific activity of immobilized enzyme was 36.67 mU.g -1 carrier with an immobilization yield of 98.87% and an enzyme recovery yield of 92.43%. The molar transformation rates of puerarin by immobilized enzyme and by the relative bacterial cell amount equal to the same amount of enzyme were 53.3% and 2.2%, respectively, after 1 hr of transformation. The former molar transformation rate, which was similar to that for free enzyme, was more than 24-fold greater than the latter. The immobilized puerarin glycosidase showed improved enzymatic properties and stability. The immobilized puerarin glycosidase retained 88% of its initial activity after being reused 10 times.

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“…Kumar et al had reported that the optimal pH of the trypsin binding to Eudragit S-100 moved to the acidic region (47). In addition, other enzymes immobilized onto the chitosan carrier have changed its optimal pH (48,49). Therefore, it shows that the difference in the micro-environmental pH is not the unique factor for influencing the optimal pH of immobilized enzymes.…”

Section: The Optimal Ph For Free and Immobilized Trypsinmentioning

confidence: 99%

Chitosan Modified PSt-GMA Microspheres With/Without Spacer-Arms as Carriers: Their Influences on Kinetics, Stability, Optimal pH, Adsorption Behavior of Immobilized Trypsin

Peng

Zhao

Liu

et al. 2012

Journal of Macromolecular Science, Part A

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A series of microspheres, chitosan modified PSt-GMA microspheres with/without the spacer-arms, have been used as carriers to study related properties about immobilized trypsin, such as isothermal adsorption, stability, kinetics and optimal reaction pH. The experimental results showed that the immobilization process could fit the Freundlich model rather than the Langmuir model, indicating the real adsorption behavior was more complex than the ideal adsorption model. In addition, K m values of trypsin immobilized onto M5 or M8 were closer to that of free enzyme and lower than that onto other microspheres, suggesting the trypsin immobilized onto M5 or M8 possessed a higher affinity to substrate. Furthermore, the thermal and operational stabilities of immobilized trypsin, particularly onto M5 or M8, were enhanced compared to that of free trypsin. Compared to free trypsin, the optimal pH of immobilized trypsin didn't change; however,its pH profile was broader. These results have proved that chitosan modified microspheres could keep the conformation and activity of enzyme as well as enhance enzyme's properties. Therefore, it has potential application in high throughput screening of drugs (HTS) based on the scintillation proximity assay (SPA) method.

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Nuclease p1 immobilized on deae cellulose

Cited by 12 publications

References 21 publications

PREPARATION AND CHARACTERIZATION OF IMMOBILIZED SPORES WITH LACCASE ACTIVITY FROM Bacillus pumilus W3 ON DEAE-CELLULOSE AND THEIR APPLICATION IN DYE DECOLORIZATION

PREPARATION AND CHARACTERIZATION OF IMMOBILIZED SPORES WITH LACCASE ACTIVITY FROM Bacillus pumilus W3 ON DEAE-CELLULOSE AND THEIR APPLICATION IN DYE DECOLORIZATION

Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Chitosan Modified PSt-GMA Microspheres With/Without Spacer-Arms as Carriers: Their Influences on Kinetics, Stability, Optimal pH, Adsorption Behavior of Immobilized Trypsin

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