Reversibility of protein denaturation is a prerequisite for all applications that depend on reliable enzyme catalysis, particularly, for using steam to sterilize enzyme reactors or enzyme sensor tips, and for developing protein-based devices that perform on-off switching of the protein function such as enzymatic activity, ligand binding and so on. In this study, we have successfully constructed...

Secretagogin is a calcium-sensor protein with six EF-hands. It is widely expressed in neurons and neuro-endocrine cells of a broad range of vertebrates including mammals, fishes and amphibia. The protein plays a role in secretion and interacts with several vesicle-associated proteins. In this work, we have studied the contribution of calcium binding and disulfide-bond formation to the stability...

Human serum albumin has been used as a model protein for protein folding and ligand binding studies over many decades. Due to its long life period and high concentration in plasma, HSA is highly sensitive to glycation. It is reported that 175 mg/dL glucose concentration is a threshold of kidney activity for the beginning of excretion of glucose. pH denaturation of HSA in absence and presence of...

The aim of this study was to analyze the effect Kanjoc oligo-glucomannan (KOG) on functional and structural changes in silver carp surimi during fluctuated (FLUC) frozen storage. During study, KOG prepared added 1 3% myofibrillar protein (MP) compared with a positive control (PC) sucrose sorbitol mixture samples. results showed that water holding capacity (WHC), textural properties decreased FL...

In prosthetic joints, frictional heating may cause protein denaturation in synovial fluid which affect its lubrication properties. arthroplasty, conventional ultra-high molecular weight polyethylene (UHMWPE) is being gradually replaced by vitamin E stabilized, extensively cross-linked UHMWPE (VEXLPE) with a superior combination of wear and oxidation resistance. There scarcity literature on vs.V...

For many years distinction has been made between acid denaturation, alkali denaturation, and the heat denaturation of proteins. In a recent review (24) heat is classified as a “physical” denaturing agent and hydrogen and hydroxyl ions as “chemical” denaturing agents. Nevertheless, it is clear that the intensity factors associated with acidity and alkalinity (the pH) and with heat (the temperatu...

Some years ago, we showed that thermo-chemically denatured, partially-unfolded forms of Pyrococcus furiosus triosephosphateisomerase (PfuTIM) display cold-denaturation upon cooling, and heat-renaturation upon reheating, in proportion with the extent of initial partial unfolding achieved. This was the first time that cold-denaturation was demonstrated for a hyperthermophile protein, following un...

Thermal stability of proteins During various industrial processes it is necessary for proteins to be temporarily placed under elevated temperatures. It is crucial to understand whether the protein of importance is stable at increased temperatures and whether the effects of increasing the temperature are reversible. The resistance of a protein to denaturation and its ability to refold are also m...

The thermal denaturation of lysozyme in aqueous alcohol solutions has been investigated through ultraviolet difference spectrophotometry and optical rotation measurements. Alcohols used were CH30H, C2H50H, and C3H70H; concentrations up to 50% (v/v) of alcohol in water were employed. It was found that upon increasing the size or the concentration of the aliphatic alcohol, the denaturation temper...