Pakistan Journal of Biological Sciences1028-88801812-5735Asian Network for Scientific Information10.3923/pjbs.2002.1077.1080KumarShaha Ranajit 102002510The surface properties of protease treated gluten were investigated with respect to their conformation changes. The helix contents of treated gluten decreased curvilinearly with its decrease of deamidation. The surface tension decreased in proportion to the degree of deamidation. On the other hand, the surface hydrophobicity of protease treated gluten increased remarkably in proportion to the degree of deamidation. The emulsifying properties of treated gluten were improved greatly by deamidation, correlating linearly with the surface hydrophobicity. From these results, the relationships between the conformational changes and functional properties of protease treated gluten are discussed.]]>Kato, A., T. Fugishing, N. Matsudomi and K. Kobashi,1983486265Kato, A. and S. Nakai,19806241320Lowry, O.H., N.J. Rosebrough, A.L. Farr and R.J. Randall,1951193265275Matsudomi, N., S. Kaneko, A. Kato and A. Kobayshi,19865019891994Nakai, S.,1983315863Pearce, K.N. and J.E. Kinsella,197826716723Shaha, R.K., N. Matsudomi and A. Kato,199731118Shaha, R.K., N.K. Sana, N. Roy, K.K. Biswas and M. Abdullah,2002Triticum aestivum L.).]]>5317320Beveridge, T., S.J. Toma and S. Nakai,1974394949Kun, E. and E.B. Kearney,1974Vol. 4,pp: 1802-1806pp: 1802-1806Naksi, S., N. Helbig, A. Kato and M.A. Tung,1980132324Shaha, R.K. and P. Hassan,20012001