Micellar enzymology: its relation to membranology

Martínek, Karel; Klyachko, Natalia L.; Kabanov, Alexander V.; Khmelnitsky, Yu. L.; Levashov, Andrey V.

doi:10.1016/0005-2736(89)90024-2

Cited by 287 publications

(167 citation statements)

References 65 publications

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“…Water release may occur upon entrapment of the molecule. In spite of the fact that experimental results state that the fixedsize model is the valid one, 119 data from other authors support the induced-fit model. Hasmann et al 120 reported that the size of BDBAC (n-benzyl-n-dodecyln-bis(2-hydroxyethyl)ammonium chloride) reversed micelles strongly increases when enzyme is placed in the core of RM.…”

Section: Reversed Micellar Systemsmentioning

confidence: 81%

“…The optimal W 0 also depends on the biomolecule concentration; the higher the concentration the higher W 0 for maximal encapsulation. 119,124,125 The pH of the solution will affect the solubilization of a protein primarily by modifying the charge distribution over the biomolecule surface. With increasing pH the protein becomes less positively charged until it reaches its isoelectric point (pI).…”

Section: Reversed Micellar Systemsmentioning

confidence: 99%

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Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Mazzola

Lopes

Hasmann

et al. 2007

J of Chemical Tech & Biotech

219

119

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Two-phase systems can be exploited in separation science for the extraction/purification of desired biomolecules. This article reviews recent experimental work on the use of aqueous two-phase polymer systems, two-phase aqueous micellar systems and reversed micellar systems for the extraction/purification of biomolecules. The experimental partitioning behavior of different biomolecules is reviewed and new results with nisin and lipopolysaccharides are presented. An extensive description of each system is presented, based on the biomolecules behavior and the tools employed to improve their extraction and purification.

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Section: Reversed Micellar Systemsmentioning

confidence: 81%

Section: Reversed Micellar Systemsmentioning

confidence: 99%

Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Mazzola

Lopes

Hasmann

et al. 2007

J of Chemical Tech & Biotech

219

119

View full text Add to dashboard Cite

show abstract

“…First, a simple nonglycosylated and well-characterized enzyme is used as the object, which permits one to vary the carbohydrate components, starting from the simpliest ones, and change their number and chemical nature. Second, the system of reversed micelles [7] is used as the reaction medium for enzymatic reactions since this system has been shown to imitate enzyme-biomembranes interactions. As a first step of this research we present here the results of a comparative study of the catalytic activity of a-chymotrypsin (ChT), native and artificially glycosylated by o-glucosamine, in reversed micelles of Aerosol OT (AOT) in octane.…”

Section: Introductionmentioning

confidence: 99%

Artificially glycosylated α‐chymotrypsin in reversed micelles of Aerosol OT in octane

et al. 1993

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A comparative study of native and artificially glycosylated achymotrypsin in reversed micelles of Aerosol OT in octane was carried out. o-Glucosamine and I-ethyl-3-(3-dimethylaminopropyl)carbodiimide were used as modifying agents to yield glycosylated enzyme. Unlike the native a-chymotrypsin, the modified protein tended to form reversible oligomeric structures, revealed by the appearance of an additional maximum (characteristic of dimeric forms of protein functioning) as a result of the enzyme catalytic activity being dependent on the AOT hydration degree. Dependence of the enzyme catalytic activity on the surfactant concentration in the case of the modified enzyme was similar to that of glycoproteins, and suggests its membrane affinity. The role of carbohydrate moieties in the functioning of glycoproteins is discussed.

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“…Most of the enzymes studied in the systems of reversed micelles exhibit a characteristic bell-shaped dependence of their catalytic activity on the degree of surfactant hydration [13][14][15][16][17]. Variations in this parameter are accompanied by changes in the size of the inner water cavity of reversed micelles [30,31].…”

Section: Resultsmentioning

confidence: 99%

“…Micellar enzymology is a novel approach to the study of the properties of biomolecules, and enzymes in particular. Its application reveals the enzyme's tendencies to form superactive conformations and supramolecular structures (reviewed in [13][14][15][16][17]). The results presented in this paper provide a new look into structure-function relationships in peroxidase catalysis.…”

Section: Introductionmentioning

confidence: 99%

Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles

Gazaryan

Klyachko

Dulkis

et al. 1997

Biochemical Journal

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Wild-type recombinant horseradish peroxidase purified and refolded from Escherichia coli inclusion bodies has been studied in the system of bis(2-ethylhexyl)sulphosuccinate sodium salt (Aerosol OT)-reversed micelles in octane. In contrast with native horseradish peroxidase the wild-type recombinant enzyme forms dimeric structures as judged by sedimentation analysis. Peroxidase substrates affect the equilibrium between monomeric and dimeric enzyme forms. The dependence of the catalytic activity of recombinant peroxidase on the degree of hydration of the surfactant exhibits two maxima with pyrogallol, o-phenylene- diamine, guaiacol and o-dianisidine, with different ratios of activities for the first and second maxima. The differences in activities of monomeric and dimeric forms of the recombinant horseradish peroxidase provide evidence for active-site screening in dimeric forms. This has been used to model a dimeric structure of recombinant horseradish peroxidase with the screened entrance to the active site. In the model structure obtained, three of eight glycosylation sites were screened. This might explain the absence of dimeric structures in native enzyme peroxidase. The system of reversed micelles provides, for the first time, evidence for the formation of dimeric structures by recombinant plant peroxidase with an altered substrate specificity compared with the native enzyme. Thus one can assume that haem-containing peroxidases in general are able to form dimeric structures.

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Micellar enzymology: its relation to membranology

Cited by 287 publications

References 65 publications

Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Artificially glycosylated α‐chymotrypsin in reversed micelles of Aerosol OT in octane

Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles

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