collagen, which is widely distributed in pluricellular animals, is one of the most fundamental constituents of the extracellular matrix, and plays mechanically or physiologically important roles in their bodies. in this study, the biochemical and physical characteristics of pepsin-solubilized collagen from the mantle of yesso scallop (ympc), a by-product of processing, was determined. electroph...

Thermal denaturation of p-Iactoglobulin type B in the absence and pteNcno: of g arious concentrations oftrehalo5e, sucrose and sork toles sugar osmolytes and twlyols were nuyoured hy monitoring changes in theabsorption coefficients at pH 2.0. These measurements gave aliss, or I. mpdpDint of denaturation), Al-fis(enthalpy change at Ty). and ACp (consttun-pressure heal capaciit eh.iltgtii under a...

Protein denaturation is considered to be the main reason for both water loss and textural changes in fish during thermal processing. Denaturation of proteins in muscle of farmed Atlantic cod was studied by differential scanning calorimetry. The denaturation of the proteins was compared to cook loss and loss in water holding capacity and it was shown that the protein denaturation occurs in a low...

thermal denaturation of a-lactalbumin in the absence and presence of various concentrations of sucrose,sorbitol, glucose and galactose as sugar osmolytes were measured by monitoring changes in the absorptions thatcarried out in a lambd 35 uv-vis double beam spectrophotometer at ph 6.0. these measurements gave valuesof t., (midpoint of denaturation), ah., (enthalpy change at t.), and acp (consta...

the thermal denaturation of adenosine deaminase (ada) has been investigated in the presence of sodium n-dodecyl sulphate (sds) over the temperature range of (293-363k) in 2.5 mm phosphate buffer, ph 6.4 by temperature scanning spectroscopy. the interaction of sds caused the folding of adenosine deaminanse resulting in a decrease of th (temperature of minimum solubility), ts (temperature of maxi...

The use of thermal denaturation of proteins prior to in-solution digestion and mass spectral peptide mass mapping is reported. Thermal denaturation is preferred over chemical denaturation because it does not require purification/concentration prior to mass spectral analysis. Enzymatic digestions of proteins that are resistant to proteolysis are significantly enhanced by thermal denaturation. Na...

OBJECTIVES The present study was designed to systematically characterize the denaturation and the renaturation of double stranded DNA (dsDNA), which is suitable for DNA hybridization. METHODS A series of physical and chemical denaturation methods were implemented on well-defined 86-bp dsDNA fragment. The degree of each denaturation was measured and the most suitable denaturation method was de...

Protein stability can be monitored by many different techniques. However, these protocols are often lengthy, consume large amounts of protein, and require expensive and specialized instruments. Here we present a new protocol to analyze protein unfolding kinetics using a quantified real-time thermocycler. This technique enables the analysis of a wide range of denaturants (and their interactions ...

Thermal denaturation of Escherichia coli maltodextrin glucosidase was studied by differential scanning calorimetry, circular dichroism (230 nm), and UV-absorption measurements (340 nm), which were respectively used to monitor heat absorption, conformational unfolding, and the production of solution turbidity. The denaturation was irreversible, and the thermal transition recorded at scan rates o...