Physicochemical characterization of the structural stability of some plant globulins

被引：32

作者：

Gorinstein, S

Zemser, M

Friedman, M

Rodrigues, WA

Martins, PS

Vello, NA

Tosello, GA

ParedesLopez, O

机构：

[1] HEBREW UNIV JERUSALEM,SCH PHARM,DEPT PHARM,IL-91120 JERUSALEM,ISRAEL

[2] UNIV SAO PAULO,INST GENET,BR-13400 SAO PAULO,BRAZIL

[3] IPN,CTR INVEST & ESTUDIOS AVANZADOS,DEPT BIOTECNOL & BIOQUIM,IRAPUATO 36500,GUANAJUATO,MEXICO

来源：

FOOD CHEMISTRY | 1996年 / 56卷 / 02期

关键词：

D O I：

10.1016/0308-8146(95)00144-1

中图分类号：

O69 [应用化学];

学科分类号：

081704 [应用化学];

摘要：

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 cu-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. Copyright (C) 1996 Elsevier Science Ltd

引用

页码：131 / 138

页数：8

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