2003
DOI: 10.1016/s0021-9797(03)00571-x
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Structure and denaturation of adsorbed lysozyme at the air–water interface

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Cited by 90 publications
(89 citation statements)
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“…Inactivation in a stirred reactor was a first order process that depended on the agitator power and the area of the various interfaces, including the gas-liquid interface (Colombie et al 2001). Postel et al (2003) suggested that the hydrophobic nature of the air-water interface caused partial deactivation of lysozyme on adsorption.…”
Section: Gas-liquid Interfacesmentioning
confidence: 99%
“…Inactivation in a stirred reactor was a first order process that depended on the agitator power and the area of the various interfaces, including the gas-liquid interface (Colombie et al 2001). Postel et al (2003) suggested that the hydrophobic nature of the air-water interface caused partial deactivation of lysozyme on adsorption.…”
Section: Gas-liquid Interfacesmentioning
confidence: 99%
“…This can be an issue in typical protein processing operations such as spray drying, where there is an increased air/solution interface. [13][14][15][16] Therefore, overall stability is a combination of factors internal and external to the protein with contributions from van der Waals interactions, electrostatic interactions, and hydrogen bonds.…”
Section: Proteins In Solution and In The Hydrated Crystalline Statementioning
confidence: 99%
“…The degree of the breakage of the globular structure of proteins upon their adsorption on a liquid surface is still intensely discussed [1][2][3][4][5][6][7][8][9][10][11]. Although the main stages of many processes in living organisms occur at interfaces and protein adsorption layers stabilize vari ous natural and industrial disperse systems, informa tion on variations in the tertiary and secondary struc tures of proteins during adsorption is extremely scarce.…”
Section: Introductionmentioning
confidence: 99%
“…Although the main stages of many processes in living organisms occur at interfaces and protein adsorption layers stabilize vari ous natural and industrial disperse systems, informa tion on variations in the tertiary and secondary struc tures of proteins during adsorption is extremely scarce. While the mechanisms of unfolding protein globules in bulk phases have been studied in detail [12], in the case of surface layers, different authors give directly opposite answers even to the main question concern ing breaking or retaining the tertiary structure of pro teins upon adsorption [1][2][3][4][5][6][7].…”
Section: Introductionmentioning
confidence: 99%
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