Protein immobilization to alumina supports: II. Papain immobilization to alumina via organophosphate linkers

Hyndman, David; Burrell, Robert E.; Lever, Gordon; Flynn, T. Geoffrey

doi:10.1002/bit.260401106

Cited by 29 publications

(10 citation statements)

References 40 publications

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“…Inorganic immobilization supports such as particulate aluminum oxides (alumina) have also been examined for immobilization of the proteolytic enzyme, papain [118]. In this research, organic phosphate linkers have been used for creation of free carboxyl groups in a two-step process.…”

Section: Immobilization Of Digestive Enzymes Onto Solid Supportsmentioning

confidence: 99%

“…It has been shown that immobilized papain had similar kinetic constants compared to papain in solution. By fluorescence measurements, it was concluded that the hydrophobic environment of the active site remained unchanged, while the structure of the rest of the protein was perturbed by its association with the negatively charged surface [118].…”

Section: Immobilization Of Digestive Enzymes Onto Solid Supportsmentioning

confidence: 99%

See 1 more Smart Citation

Enzyme immobilization: an update

et al. 2013

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Compared to free enzymes in solution, immobilized enzymes are more robust and more resistant to environmental changes. More importantly, the heterogeneity of the immobilized enzyme systems allows an easy recovery of both enzymes and products, multiple re-use of enzymes, continuous operation of enzymatic processes, rapid termination of reactions, and greater variety of bioreactor designs. This paper is a review of the recent literatures on enzyme immobilization by various techniques, the need for immobilization and different applications in industry, covering the last two decades. The most recent papers, patents, and reviews on immobilization strategies and application are reviewed.

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Section: Immobilization Of Digestive Enzymes Onto Solid Supportsmentioning

confidence: 99%

Section: Immobilization Of Digestive Enzymes Onto Solid Supportsmentioning

confidence: 99%

Enzyme immobilization: an update

et al. 2013

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“…Several strategies have been devised for enhancing the stability and activity of enzymes in organic media, such as chemical modification, 3 immobilization, 4,5 molecular imprinting with substrates, 6 the addition of effectors, 7 and the use of surfactants. 8,9 Substantial attention has been devoted to the covalent immobilization of enzymes to porous, insoluble supports such as glass, 10 alumina, 11 silica, 11 and chitosan [12][13][14][15][16][17][18][19][20][21] because they possess a high catalytic activity per unit volume of the catalyst and minimum diffusion limitations and facilitate the diffusion of large substrate molecules into the porous structure of the matrix within which enzymes are bound.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of horseradish peroxidase on chitosan for use in nonaqueous media

Bindhu

Abraham

2003

J of Applied Polymer Sci

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Chitosan, a natural polysaccharide, was used for the covalent immobilization of horseradish peroxidase, an enzyme of high synthetic utility, with the carbodiimide method. Of the enzyme, 62% was immobilized on chitosan when 1-ethyl-3-(3-dimethylaminopropyl carbodiimide) was used as the peptide coupling agent. The influence of different parameters, such as the enzyme concentration, carbodiimide concentration, and incubation period, on the activity retention of the immobilized enzyme was investigated. Kinetic studies using horseradish peroxidase immobilized on chitosan revealed the effects of several parameters, such as the substrate hydrophilicity and hydrophobicity, the solubility of substrates in the medium, the solvent hydrophobicity, and the support aquaphilicity, on the catalytic activity of the immobilized enzyme in nonaqueous media. General rules for the optimization of solvents for nonaqueous enzymology based on the partitioning of the solvent were not applicable for the immobilized horseradish peroxidase. The catalytic efficiency was greatest when o-phenylene diamine was used as the substrate and least when guaiacol was used. The aquaphilicity of the support played an important role in the kinetics of the immobilized horseradish peroxidase in water-miscible solvents. The results were promising for the future development of chitosan-immobilized enzymes for use in organic media.

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“…Papain has known to work effectively when immobilized in other different supports like on SiO 2 particles containing amine groups [8], alumina [9], nitrilon fiber carrier [10], and water soluble polymer polyvinyl alcohol [11]. Additionally, it is expected that an aerosol spray with formulated papain in pectin gel would not cause any drip.…”

Section: Introductionmentioning

confidence: 99%

“…In weight/volume terms, the enzyme preparations are seldom pure and it is expected that the enzyme source will be used in amounts from 0.001% by weight to 20% by weight formulation. Precise amounts will vary with purity of the enzyme [8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

A new formulated stable papin-pectin aerosol spray for skin wound healing

Jáuregui

Cabrera

Ceniceros

et al. 2009

Biotechnol Bioproc E

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^Äëíê~Åí= A new spray-on topical wound debrider composition consisting of 0.1% w/v papain immobilized in 6% w/v pectin gel was formulated for skin wound healing. The stability of the enzyme activity of this new formulated spray was compared with the 0.1% w/v papain in water solution at the refrigerated temperature of 4 and 75°C. Two aerosol propellants, air and nitrogen, were evaluated for their efficacy. The new formulated spray was then evaluated for its thermal stability under air and N 2 at 75°C. All enzyme activity of papain was measured with a spectrophotometer using casein as a substrate at 37°C and in 0.1 M phosphate buffer at pH 6, as well as trichloral acetic acid to separate the product of casein hydrolysis. All the evaluations showed the new aerosol spray formulation to be far better than the liquid formulation in storage stability and thermal stability at 75°C under atmospheric or higher pressures. The new formulation was tested in a rabbit experiment to evaluate the effectiveness of wound healing. As compared to untreated wound, the formulated spray clearly was superior, yielding a 20% more healing progress in the first 4 days alone. © KSBB hÉóïçêÇëW=é~é~áå=ëí~ÄáäáíóI=éÉÅíáå=ÖÉäI=éêçéÉää~åí=éêÉëëìêÉ=ÉÑÑÉÅí

show abstract

Protein immobilization to alumina supports: II. Papain immobilization to alumina via organophosphate linkers

Cited by 29 publications

References 40 publications

Enzyme immobilization: an update

Enzyme immobilization: an update

Immobilization of horseradish peroxidase on chitosan for use in nonaqueous media

A new formulated stable papin-pectin aerosol spray for skin wound healing

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