Hydration and thermal denaturation of β-lactoglobulin. A calorimetric study

Rüegg, Max; Moor, U.; Blanc, B.

doi:10.1016/0005-2795(75)90188-9

Cited by 79 publications

(24 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This indicates that these proteins are resistant to heat treatment in the dry state, which was demonstrated earlier for dry proteins in general by other methods (Ruegg et al, 1975;Fujita and Noda, 1978). However, as expected for hydrated proteins (Ismail et al, 1992;Arrondo et al, 1994), in fully hydrated pollen the proteins are denatured when they are heated at 100°C for 5 or 10 min (Fig.…”

Section: Protein Structure In Denatured Pollenmentioning

confidence: 82%

Aging of Dry Desiccation-Tolerant Pollen Does Not Affect Protein Secondary Structure

Wolkers

Hoekstra²

1995

Plant Physiol.

View full text Add to dashboard Cite

Protein secondary structure and membrane phase behavior i n aging Jypha latifolia pollen were studied by means of Fourier transform infrared microspectroscopy (FTIR). Membranes isolated from fresh pollen occurred mainly in the liquid crystalline phase at room temperature, whereas the membrane fluidity of aged pollen was drastically decreased. This decrease did not result i n large-scale irreversible protein aggregation, as was concluded from i n situ FTIR assessment of the amide-1 bands. Curve-fitting on the infrared absorbance spectra enabled estimation of the proportion of different classes of protein secondary structure. Membrane proteins had a relatively large amount of a-helical structure (48%; band at 1658 cm-'1, and turn-like structures (at 1637 and 1680 cm-') were also detected. The secondary protein structure of isolated cytoplasmic proteins resembled that of proteins in whole pollen and was conserved upon drying in the absence of sucrose. The isolated cytoplasmic proteins had a large amount of a-helical structure (43%), and also P-sheet (at 1637 and 1692 cm-') and turn structures were detected. Heat-denaturing experiments with intact hydrated pollen showed low (1627 cm-') and high (1692 cm-') wave number bands indicating irreversible protein aggregates. The results presented in this paper show that FTIR is an extremely suitable technique to study protein secondary structure in intact plant cells of different hydration levels and developmental stages.Cattail (Typka latifolia) pollen can be dried to water contents of less than 0.05 g H,O g-' dry weight without losing viability. In an atmosphere of 40% RH the pollen attains about 0.06 g H,O g-' dry weight and has a maximum life span of approximately 120 d at 24°C in the dark (van Bilsen and Hoekstra, 1993). At the higher RH of 75% the water content increases to approximately 0.20 g H,O g-' dry

show abstract

Section: Protein Structure In Denatured Pollenmentioning

confidence: 82%

Aging of Dry Desiccation-Tolerant Pollen Does Not Affect Protein Secondary Structure

Wolkers

Hoekstra²

1995

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…Eqn [3] where D r = decimal reduction time at a reference temperature (min), T = temperature (K), T r = a reference temperature (K), z = z value (°C or K), defined as the temperature increase needed to reduce the D-value by one log unit. The reference temperature used was 140°C (413 K).…”

Section: Discussionmentioning

confidence: 99%

“…There are two methods for estimating the model parameters in both cases: one-step and two-step. With the one-step method, all inactivation data are fitted to Eqn [1], after applying Eqn [3] (or [4]) to express the temperature dependency of the rate constant, using a non linear regression. The two-step method consists of fitting the results of each isothermal experiment with Eqn [1] to obtain rate constants at different temperatures, which are then fitted to [3] (or [4]).…”

Section: Discussionmentioning

confidence: 99%

Analysis of the Inactivation Kinetics of Freeze-dried α-Amylase fromBacillus amyloliquefaciensat Different Moisture Contents

Saraiva

Oliveira

Hendrickx

et al. 1996

LWT - Food Science and Technology

View full text Add to dashboard Cite

show abstract

“…Properties of water in biological systems were studied extensively using isothermal sorption measurement (Schneider and Schneider, 1972;Clegg, 1978;Lusher-Mattli and Ruegg, 1982;Rupley et al, 1983), calorimetric method (Ruegg et al, 1975;Bakradze and Balla, 1983;Vertucci, 1990), infrared and Raman spectroscopy (Careri et al, 1979;Luck, 1985;Cameron et al, 1988), nuclear magnetic resonance (NMR) spectroscopy (Mathur-de Vre, 1979;Seewaldt et al, 1981;Rorschach and Hazlewood, 1986;Ratkovic, 1987), quasi-elastic neutron-scattering spectroscopy (Lehmann, 1984;Trantham et al, 1984), and dielectric relaxation techniques (Harvey and Hoekstra, 1972;Kamiyoshi and Kudo, 1978;Clegg et al, 1982;Pissis et al, 1987;Bruni and Leopold, 1992;Pissis et al, 1996). These studies revealed the great structural complexity of water in biological systems.…”

mentioning

confidence: 99%

Dielectric Relaxation of Water and Water-Plasticized Biomolecules in Relation to Cellular Water Organization, Cytoplasmic Viscosity, and Desiccation Tolerance in Recalcitrant Seed Tissues

Sun

2000

Plant Physiology

View full text Add to dashboard Cite

To understand the relationship between the organization of cellular water, molecular interactions, and desiccation tolerance, dielectric behaviors of water and water-plasticized biomolecules in red oak (Quercus rubra) seeds were studied during dehydration. The thermally stimulated current study showed three dielectric dispersions: (a) the relaxation of loosely-bound water and small polar groups, (b) the relaxation of tightly-bound water, carbohydrate chains, large polar groups of macromolecules, and (c) the "freezing in" of molecular mobility (glassy state). Seven discrete hydration levels (water contents of 1.40, 0.55, 0.41, 0.31, 0.21, 0.13, and 0.08 g/g dry weight, corresponding to Ϫ1.5, Ϫ8, Ϫ11, Ϫ14, Ϫ24, Ϫ74, and Ϫ195 MPa, respectively) were identified according to the changes in thermodynamic and dielectric properties of water and water-plasticized biomolecules during dehydration. The implications of intracellular water organization for desiccation tolerance were discussed. Cytoplasmic viscosity increased exponentially at water content Ͻ 0.40 g/g dry weight, which was correlated with the great relaxation slowdown of water-plasticized biomolecules, supporting a role for viscosity in metabolic shutdown during dehydration.

show abstract

Hydration and thermal denaturation of β-lactoglobulin. A calorimetric study

Cited by 79 publications

References 24 publications

Aging of Dry Desiccation-Tolerant Pollen Does Not Affect Protein Secondary Structure

Aging of Dry Desiccation-Tolerant Pollen Does Not Affect Protein Secondary Structure

Analysis of the Inactivation Kinetics of Freeze-dried α-Amylase fromBacillus amyloliquefaciensat Different Moisture Contents

Dielectric Relaxation of Water and Water-Plasticized Biomolecules in Relation to Cellular Water Organization, Cytoplasmic Viscosity, and Desiccation Tolerance in Recalcitrant Seed Tissues

Contact Info

Product

Resources

About