Physicochemical characterization of the structural stability of some plant globulins

S. Gorinstein; M. Zemser; M. Friedman; W. A. Rodrigues; P. S. Martins; N. A. Vello; G. A. Tosello; O. Paredes-López

doi:10.1016/0308-8146(95)00144-1

Physicochemical characterization of the structural stability of some plant globulins

S. Gorinstein^*, M. Zemser, M. Friedman, W. A. Rodrigues, P. S. Martins, N. A. Vello, G. A. Tosello, O. Paredes-López

^*Corresponding author for this work

School of Pharmacy

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

The fluorescence properties of amaranth, soybean, rice, sorghum and maize globulins, and cassava globulin-like proteins were measured as a function of fluorescent light intensity, peak response and shift in the maximum of emission using the fluorescence of tryptophan at 295 nm. Application of differential scanning calorimetry (DSC) of these globulins gave a quantitative estimation of their thermal stabilities in solid state. The thermodynamic data associated with transition and the number of ruptured hydrogen bonds were calculated. Differences in secondary structure and α-helical content were observed. Relative structural stabilities of native plant globulins were also estimated by X-ray diffractometry and Fourier transform infrared (FT-IR) measurements.

Original language	English
Pages (from-to)	131-138
Number of pages	8
Journal	Food Chemistry
Volume	56
Issue number	2
DOIs	https://doi.org/10.1016/0308-8146(95)00144-1
State	Published - Jun 1996

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title = "Physicochemical characterization of the structural stability of some plant globulins",

abstract = "The fluorescence properties of amaranth, soybean, rice, sorghum and maize globulins, and cassava globulin-like proteins were measured as a function of fluorescent light intensity, peak response and shift in the maximum of emission using the fluorescence of tryptophan at 295 nm. Application of differential scanning calorimetry (DSC) of these globulins gave a quantitative estimation of their thermal stabilities in solid state. The thermodynamic data associated with transition and the number of ruptured hydrogen bonds were calculated. Differences in secondary structure and α-helical content were observed. Relative structural stabilities of native plant globulins were also estimated by X-ray diffractometry and Fourier transform infrared (FT-IR) measurements.",

author = "S. Gorinstein and M. Zemser and M. Friedman and Rodrigues, {W. A.} and Martins, {P. S.} and Vello, {N. A.} and Tosello, {G. A.} and O. Paredes-L{\'o}pez",

year = "1996",

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doi = "10.1016/0308-8146(95)00144-1",

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T1 - Physicochemical characterization of the structural stability of some plant globulins

AU - Gorinstein, S.

AU - Zemser, M.

AU - Friedman, M.

AU - Rodrigues, W. A.

AU - Martins, P. S.

AU - Vello, N. A.

AU - Tosello, G. A.

AU - Paredes-López, O.

PY - 1996/6

Y1 - 1996/6

N2 - The fluorescence properties of amaranth, soybean, rice, sorghum and maize globulins, and cassava globulin-like proteins were measured as a function of fluorescent light intensity, peak response and shift in the maximum of emission using the fluorescence of tryptophan at 295 nm. Application of differential scanning calorimetry (DSC) of these globulins gave a quantitative estimation of their thermal stabilities in solid state. The thermodynamic data associated with transition and the number of ruptured hydrogen bonds were calculated. Differences in secondary structure and α-helical content were observed. Relative structural stabilities of native plant globulins were also estimated by X-ray diffractometry and Fourier transform infrared (FT-IR) measurements.

AB - The fluorescence properties of amaranth, soybean, rice, sorghum and maize globulins, and cassava globulin-like proteins were measured as a function of fluorescent light intensity, peak response and shift in the maximum of emission using the fluorescence of tryptophan at 295 nm. Application of differential scanning calorimetry (DSC) of these globulins gave a quantitative estimation of their thermal stabilities in solid state. The thermodynamic data associated with transition and the number of ruptured hydrogen bonds were calculated. Differences in secondary structure and α-helical content were observed. Relative structural stabilities of native plant globulins were also estimated by X-ray diffractometry and Fourier transform infrared (FT-IR) measurements.

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JF - Food Chemistry

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Physicochemical characterization of the structural stability of some plant globulins

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