Probing the Bovine Hemoglobin Adsorption Process and its Influence on Interfacial Water Structure at the Air–Water Interface

* These authors contributed equally to this work. The molecular-level insight of protein adsorption and its kinetics at interfaces is crucial because of its multifold role in diverse fundamental biological processes and applications. In the present study, the sum frequency generation (SFG) vibrational spectroscopy has been employed to demonstrate the adsorption process of bovine hemoglobin (BHb) protein molecules at the air–water interface at interfacial isoelectric point of the protein. It has been observed that surface coverage of BHb molecules significantly influences the arrangement of the protein molecules at the interface. The time-dependent SFG studies at two different frequencies in the fingerprint region elucidate the kinetics of protein denaturation process and its influence on the hydrogen-bonding network of interfacial water molecules at the air–water interface. The initial growth kinetics suggests the synchronized behavior of protein adsorption process with the structural changes in the interfacial water molecules. Interestingly, both the events carry similar characteristic time constants. However, the conformational changes in the protein structure due to the denaturation process stay for a long time, whereas the changes in water structure reconcile quickly. It is revealed that the protein denaturation process is followed by the advent of strongly hydrogen-bonded water molecules at the interface. In addition, we have also carried out the surface tension kinetics measurements to complement the findings of our SFG spectroscopic results.

THE STUDY OF THERMAL DENATURATION OF BEEF, PORK, CHICKEN AND TURKEY MUSCLE PROTEINS USING DIFFERENTIAL SCANNING CALORIMETRY

In the temperature range from 45 °C to 90 °C the process of thermal denaturation of a whole complex of muscle proteins in meat takes place. An effective mode to register the thermal denaturation process is the method of differential scanning calorimetry (DSC). As a result of studies the differences during the process of thermal denaturation of muscle proteins of pork, beef, chicken and turkey were defined by the appearance of endothermic peaks in DSC thermograms. The main variances are associated with the process of denaturation of myosin and sacroplasmic proteins and indicate indirectly their quantitative ratio in meat. The values of effective specific heat capacity in the temperature range from 20 °C to 90 °C are obtained as well as those of heat spent on the denaturation process.At reheating, the values of specific heat capacity increased by 0.1 J/(g*K) on the average, and peaks of thermal denaturation were not detected, that certifies the irreversibility of the denaturation process and the decrease in the bound moisture proportion in meat after thermal processing. Knowledge of the nature of protein thermal denaturation of each kind of meat product is one of the necessary tools for developing the technology of meat product thermal processing.

Molecular mechanism for thermal denaturation of thermophilic rhodopsin

Studies of microbial rhodopsins revealed that hydrolysis of the retinal protonated Schiff base is the rate-determining step of the thermal denaturation process.

Kinetic and thermodynamic parameters for heat denaturation of human recombinant lactoferrin from rice1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.

Heat denaturation of recombinant human lactoferrin (rhLf) from rice with 3 different iron-saturation degrees, holo rhLf (iron-saturated), AsIs rhLf (60% iron saturation), and apo rhLf (iron-depleted), was studied. The 3 forms of rhLf were subjected to heat treatment, and the kinetic and thermodynamic parameters of the denaturation process were determined. Thermal denaturation of rhLf was assessed by measuring the loss of reactivity against specific antibodies. Dt values (time to reduce 90% of immunoreactivity) decreased with increasing temperature of treatment for apo and holo rhLf, those values being higher for the iron-saturated form, which indicates that iron confers thermal stability to rhLf. However, AsIs rhLf showed a different behaviour with an increase in resistance to heat between 79 °C and 84 °C, so that the kinetic parameters could not be calculated. The heat denaturation process for apo and holo rhLf was best described assuming a reaction order of 1.5. The activation energy of the denaturation process was 648.20 kJ/mol for holo rhLf and 406.94 kJ/mol for apo rhLf, confirming that iron-depleted rhLf is more sensitive to heat treatment than iron-saturated rhLf.

On the Information Problem of DNA in the Denaturation Process

The information problem of DNA in the denaturation process was studied by the relationship between entropy and information. Using the previous PB’s (Peyrard and Bishop) numerical results obtained from their microscopic arharmonic model of DNA, we propose a new effective simple model to calculate DNA information. A shape change of information at the denaturation phase transition point was found and discussed.