Immobilization of peroxidases on glass beads: An improved alternative for phenol removal

Gómez, José L.; Bódalo, A.; Gómez, E.; Bastida, Jaume; Hidalgo, A.M.; Gómez, M.

doi:10.1016/j.enzmictec.2006.02.008

Cited by 152 publications

(74 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This allows the biocatalyst to survive longer during process conditions and allows one to operate the process at higher temperature [3]. There are many immobilization techniques available such as adsorption [4], covalent attachment [5] and entrapment [6]. Non-covalent binding processes are simple but have the disadvantage of weak binding of enzyme.…”

Section: Introductionmentioning

confidence: 99%

Studies on the activity and stability of immobilized horseradish peroxidase on poly(ethylene terephthalate) grafted acrylamide fiber

Temoçin

Yi̇ği̇toğlu

2008

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

Having been activated with glutaraldehyde, modified poly(ethylene terephthalate) grafted acrylamide fiber was used for the immobilization of horseradish peroxidase (HRP). Both the free HRP and the immobilized HRP were characterized by determining the activity profile as a function of pH, temperature, thermal stability, effect of organic solvent and storage stability. The optimum pH values of the enzyme activity were found as 8 and 7 for the free HRP and the immobilized HRP respectively. The temperature profile of the free HRP and the immobilized HRP revealed a similar behaviour, although the immobilized HRP exhibited higher relative activity in the range from 50 to 60 degrees C. The immobilized HRP showed higher storage stability than the free HRP.

show abstract

Section: Introductionmentioning

confidence: 99%

Studies on the activity and stability of immobilized horseradish peroxidase on poly(ethylene terephthalate) grafted acrylamide fiber

Temoçin

Yi̇ği̇toğlu

2008

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

show abstract

“…Other popular enzymes are horseradish peroxidase and soybean peroxidase: Both enzymes were covalently immobilized onto aldehyde glass through their amine groups, and a clear protective effect of the immobilization against the enzyme inactivation by hydrogen peroxide was found [257,258].…”

Section: Improved Rigidity Of the Enzymementioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

140

107

View full text Add to dashboard Cite

Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

show abstract

“…Novel research in the area of enzyme technology has provided significant evidence and strategies that facilitate using enzymes optimally at large scale by entrapping and immobilizing [14,15]. Although enzymes entrapped in porous polymeric matrices pose inherent limitations of enzyme leaching; however by controlling the pore dimensions such leaching can be minimized.…”

Section: Introductionmentioning

confidence: 99%

Application of Immobilized Pointed Gourd (Trichosanthes dioica) Peroxidase-Concanavalin A Complex on Calcium Alginate Pectin Gel in Decolorization of Synthetic Dyes Using Batch Processes and Continuous Two Reactor System

Jamal¹

2013

J Bioproces Biotechniq

View full text Add to dashboard Cite

Ammonium sulphate fractionated pointed gourd (Trichosanthes dioica) peroxidase-concanavalin A (PGP-Con A) complex was entrapped into calcium alginate-pectin gel. Catalytic performance of immobilized PGP-Con A complex in dye decolorization was examined on repeated use and reusing after a prolonged period of storage. Immobilized and entrapped peroxidase preparation retained 59.6% of the original activity after a period of 50 d. Entrapped PGPCon A complex decolorized 91.2% and 82.1% of the initial color from DR19 and dye mixture [DR19+DB9] after 20 d, respectively. Considerable color removal was found even after 120 d and 80 d respectively, of operation of two reactor system and total organic carbon analysis was quite comparable to color loss. This study shows the efficacy, durability and sustainability of using immobilized T. dioica peroxidase in batch and continuous two reactor catalytic system for the removal of synthetic dyes from industrial effluents.

show abstract

Immobilization of peroxidases on glass beads: An improved alternative for phenol removal

Cited by 152 publications

References 29 publications

Studies on the activity and stability of immobilized horseradish peroxidase on poly(ethylene terephthalate) grafted acrylamide fiber

Studies on the activity and stability of immobilized horseradish peroxidase on poly(ethylene terephthalate) grafted acrylamide fiber

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Application of Immobilized Pointed Gourd (Trichosanthes dioica) Peroxidase-Concanavalin A Complex on Calcium Alginate Pectin Gel in Decolorization of Synthetic Dyes Using Batch Processes and Continuous Two Reactor System

Contact Info

Product

Resources

About