Adsorption of Invertase.

Nelson, J. M.; Griffin, Edward G.

doi:10.1021/ja02262a018

Cited by 269 publications

(108 citation statements)

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“…[58] The aim of immobilization is to maintain the catalytic activity of the enzyme whilst improving its stability and ease of recovery and reuse. Numerous methods of immobilizing enzymes on a wide variety of supports have been studied.…”

Section: Immobilization Of Proteins In Mpsmentioning

confidence: 99%

Proteins in Mesoporous Silicates

2008

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Mesoporous silicates (MPS) have an ordered pore structure with dimensions comparable to many biological molecules. They have been extensively explored as supports for proteins and enzymes in biocatalytic applications. Since their initial discovery, novel syntheses methods have led to precise control over pore size and structure, particle size, chemical composition, and stability, thus allowing the adsorption of a wide variety of biological macromolecules, such as heme proteins, lipases, antibody fragments, and proteases, into their structures. This Review discusses the application of ordered, large-pore, functionalized mesoporous silicates to immobilize proteins for biocatalysis.

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Section: Immobilization Of Proteins In Mpsmentioning

confidence: 99%

Proteins in Mesoporous Silicates

2008

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“…Nelson and Griffin reported the first physical adsorption of invertase. 20 We focused on the physical adsorption of hTM onto a polymeric biomaterial surface because physical adsorption can prevent denaturation and leaves no remnant chemical reagents. The physical adsorption of hTM onto biomaterial surfaces is expected to generate safe antithrombogenic blood-contacting materials.…”

Section: Introductionmentioning

confidence: 99%

Physical adsorption of human thrombomodulin (ART‐123) onto polymeric biomaterials for developing an antithrombogenic blood‐contacting material

Matsusaki

Omichi

Maruyama

et al. 2007

J Biomedical Materials Res

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Human thrombomodulin (hTM) is an endothelial cell-associated protein with potent natural anticoagulant activity by converting thrombin from a procoagulant protease to an anticoagulant. ART-123 is a recombinant soluble hTM (amino acid residues 1-498), and we focused on the physical adsorption of ART-123 onto a polymeric biomaterial surface to develop an antithrombogenic blood-contacting material with preventing the denaturation of hTM and the remaining chemical reagents. The adsorption of hTM onto polysulfone (PSF) films was analyzed quantitatively by quartz crystal microbalance analysis. The adsorption constant and the maximum adsorption amount, calculated by the assumption of a Langmuir-type adsorption, showed that hTM adsorbed with a relatively weak interaction onto the PSF film. The hydrophilic protein lysozyme also showed a Langmuir-type monolayer adsorption, although hydrophobic catalase and fibrinogen showed multilayer adsorption accompanying the denaturation. The physically adsorbed hTM showed high coenzymatic activity for the activation of protein C, as well as anticoagulant activity. Furthermore, the surface wettability of the PSF film was easily controllable by the physical adsorption of hydrophobic and hydrophilic bioactive proteins. The physical adsorption of hTM or bioactive proteins onto polymeric biomaterials will be instrumental for developing an antithrombogenic blood-contacting biomaterial, and for controlling the surface properties of biomaterials.

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“…Microbial films developed on the shavings and converted the ethanol to acetic acid ("Quick" process, invented in 1823). Attempts to immobilize enzymes date back as far as 1916, when Nelson and Griffin showed that immobilized invertase was active [5].…”

Section: Introductionmentioning

confidence: 99%

“…Table 1. Historical development of immobilized biocatalysts (partly based on [6]) Year Biocatalyst, process, or event Comments 1823 vinegar manufacture from alcoholic solutions by using biofilm on wood chips ("Quick" process) 1916 invertase adsorbed on charcoal [5] 1948 urease insolubilization [7] 1949 physiologically active protein immobilization [8] 1951 albumin bound to diazonium derivative of 4-aminobenzyl cellulose [9] 1953 immobilization of carboxypeptidase, diastase, pepsin, and ribonuclease [10] 1969 continuous optical resolution of d,l-amino acids by immobilized aminoacylase [11] first industrial process employing an immobilized biocatalyst 1971 First Enzyme Engineering Conference at Henniker, New Hampshire [12] definition of immobilized enzymes 1972 isomerization of glucose to fructose by immobilized glucose isomerase [13] 1973 production of l-aspartic acid by immobilized Escherichia coli (aspartase) [14] first industrial use of immobilized microbial cells 1975 adsorption of rat liver mitochondria on alkylsilanized glass beads [15] first immobilization of subcellular particles 1979 adsorption of algae (Anabaena cylindrica) on glass beads for the evolution of hydrogen [16] [17] first immobilization of plant cells 1979 slice of porcine kidney immobilized in the membrane of an ammonia electrode for amino acid detection [18] first immobilization of animal cells…”

Section: Introductionmentioning

confidence: 99%