Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus) |
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| Institution: | 1. Laboratoire Réactions et Génie des Procédés, Université de Lorraine, CNRS, LRGP, F-54000 Nancy, France;2. Université de Lorraine, 2 Avenue de la forêt de Haye, F-54505 Vand?uvre-lès-Nancy, France;3. Avril SCA, 11 rue de Monceau, F-75008 Paris, France;1. Centro Tecnológico de la Carne de Galicia, Avda. Galicia n° 4, Parque Tecnológico de Galicia, San Cibrao das Viñas 32900, Ourense, Spain;2. Department of Food Engineering, Faculty of Animal Science and Food Engineering, University of São Paulo, 225 Duque de Caxias Norte Ave, Jardim Elite, 13.635-900, Pirassununga, São Paulo, Brazil;3. Área de Tecnología de los Alimentos, Facultad de Ciencias de Ourense, Universidad de Vigo, 32004, Ourense, Spain |
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| Abstract: | Mullet (Mugil cephalus) muscle homogenates were adjusted to different pH ranging from 2 to12 and the proteins extracted were evaluated for changes in solubility and conformational characteristics viz. surface hydrophobicity and reactive sulphydryl groups. Altering the pH of muscle homogenate to acidic or alkaline increased protein solubility. The hydrophobicity of the proteins increased on exposure to extreme pH indicating unfolding. The reactive sulphydryl groups decreased at acidic and alkaline pH with the lowest at pH 4. When the pH of the muscle homogenates was brought back to the original pH (6.3), the protein solubility was found to decrease. Reactive sulphydryl groups and ANS hydrophobicity of the proteins increased on readjusting the pH resulting in a molten-globule state. The electrophortogram of the samples corresponded well with the observations. Alterations in functional properties of these modified proteins are an area of interest for commercial application. |
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