1999
DOI: 10.1002/(sici)1097-0290(19990805)64:3<373::aid-bit14>3.0.co;2-j
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Activity losses among T4 lysozyme charge variants after adsorption to colloidal silica

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Cited by 29 publications
(30 citation statements)
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“…Proteins, including lysozyme, horseradish peroxidase, catalase, and trypsin, adsorb strongly to SiO 2 (sizes ranging from 9 to 40 nm) nanoparticles. These proteins undergo a partial loss of structure and generally a significant loss in enzyme activity (Norde and Anusiem 1992;Kondo et al 1993;Bower et al 1998;Czeslik and Winter 2001).…”
Section: Nanosilica For Medicine and Drug Developmentmentioning
confidence: 99%
“…Proteins, including lysozyme, horseradish peroxidase, catalase, and trypsin, adsorb strongly to SiO 2 (sizes ranging from 9 to 40 nm) nanoparticles. These proteins undergo a partial loss of structure and generally a significant loss in enzyme activity (Norde and Anusiem 1992;Kondo et al 1993;Bower et al 1998;Czeslik and Winter 2001).…”
Section: Nanosilica For Medicine and Drug Developmentmentioning
confidence: 99%
“…We used a number of techniques to study the interfacial behavior of charge-changed as well as structural stability mutants of T4 lysozyme, including in situ ellipsometry [20][21][22][23][24], air-water interfacial tensiometry [25,26], radioisotope labeling with 125 I [24] and 14 C [26], circular dichroism (CD) [27,28], the interferometric surface force technique [29], and various assays of enzymatic activity of T4 lysozyme mutants bound to surfaces [30,31]. The elution of adsorbed protein by surfactant had been used by Horbett and coworkers [32][33][34][35][36] to provide an index of protein binding strength, and the earliest work with T4 lysozyme at interfaces was focused on ellipsometric detection of the adsorption and dodecyltrimethylammonium bromide-mediated elution of T4 lysozyme stability variants at hydrophilic and hydrophobic surfaces [20].…”
Section: Measurement Of Protein Adsorption and Binding Strengthmentioning
confidence: 99%
“…Bower et al [30,31] correlated the changes in secondary structure that occurred among T4 lysozyme variants with their corresponding changes in enzymatic activity using two different assays. In one, lyophilized Micrococcus lysodeikticus cells were suspended in phosphate buffer, and the activities of T4 lysozyme as well as T4 lysozyme-nanoparticle complexes were determined by measuring the decrease in turbidity of the Micrococcus substrate as a function of time.…”
Section: Measurement Of Adsorbed T4 Lysozyme Functionmentioning
confidence: 99%
“…Lower and coworkers [199] have investigated the adsorption of T4 lysozyme on colloidal silica. It was observed that the enzymatic activity decreased upon adsorption due to the differences in adsorbed enzyme structure and orientation as well as the electrostatic effects.…”
Section: Immobilization In Siomentioning
confidence: 99%