1990
DOI: 10.1002/abio.370100122
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Nonionic tensides modify papain structure and proteolytic activity

Abstract: The effect of 33 polyethoxylated nonionic tensides with various hydrophobic moieties was studied on the proteolytic activity and phase transition behaviour of papain. Tensides with longer ethyleneoxide chain markedly increased the phase transition temperatures of papain indicating possible hydrogen bond formation between the hydrophilic ethyleneoxide chain and the polar substructures of papein. The character of Iipophilic moiety of tensides influences also each physicochemical parameter of papain suggesting th… Show more

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Cited by 6 publications
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“…Nonhomologous series of nonionic surfac-tants increased the activity of papain and modified its structure as determined by differential scanning calorimetry. Both the hydrophobic and hydrophilic molecular characteristics of surfactants influenced their effect on the activity and structure of papain (55). In contrast, similar surfactants markedly inhibited the activity of horseradish peroxidase.…”
mentioning
confidence: 99%
“…Nonhomologous series of nonionic surfac-tants increased the activity of papain and modified its structure as determined by differential scanning calorimetry. Both the hydrophobic and hydrophilic molecular characteristics of surfactants influenced their effect on the activity and structure of papain (55). In contrast, similar surfactants markedly inhibited the activity of horseradish peroxidase.…”
mentioning
confidence: 99%