High Hydrostatic Pressure (HHP) High hydrostatic pressure is a non-thermal technique that’s been used since the late 1800s to process foods (Hite, 1899). Its use in large scale processing only began in the last 20 years, due to innovation of new technologies that allowed the construction of high pressure chambers that could withstand the high pressures that the process requires at a reasonable price (Muntean et al., 2016). To work, HHP requires the adjustment of three parameters: temperature, pressure, and exposure time. It works under two principles: 1. Le Chatelier’s principle: if pressure is applied to a system that is in equilibrium, molecules within that system will react to offset that pressure until equilibrium is re-established. These reactions will result in the inactivation of microorganisms and enzymes. 2. Isostatic rule: when pressure is applied to food products, they will compress regardless of the size and geometry of the product. (Chawla, Patil, & Singh, 2011) This process disrupts non-covalent bonds, such as ionic, hydrogen and hydrophobic bonds, due to their susceptibility to pressure. HHP does not affect vitamins and aromatic compounds due to their low molecular weight (Carlez, Rosec, Richard, & Cheftel, 1994). In the case of larger molecules, such as proteins, their structure is lengthened after HHP treatment, which in essence destroys the 3D structure of the large molecule, thus changing the structure of a protein or in the case of enzymes,
The following experiment was conducted to investigate the effect of concentration on a potato core. The experiment was done see whether or not the concentration in the NaCl solution would effect the mass of a piece of potato core, the experiment briefly showed that each concentration of NaCl decreased the mass of the piece of potato.
The effect that increasing Na+Cl- concentration had on osmotic pressure was that the pressure also
Background Information: We are going to use our knowledge of the Le Chatelier’s principle in order to observe this experiment. The principle states that the equilibrium will shift in the direction that will minimize the effects of the change.
The objective of the experiment is to apply Le Chatelier's Principle, which is a system that responds to an external stress and then adjusts itself in order to alleviate the stress when it is at equilibrium. A reactant is added, and the equilibrium is reestablished, resulting in more products and fewer reactants, and thus, the position of equilibrium is shifted to the right. When a product is added, the equilibrium position is shifted to the left because there are more reactants and fewer products.
Hydrogen bonds contribute to a property of water called cohesion or the tendency of water molecules to stick together.
Regarding temperature, Le Chatelier’s principle states that seeing as the production of COCl2 from CO + Cl2 comes about through a process of exothermic reaction, that the reverse would come about through a process of endothermic reaction. Therefore increasing the temperature would cause a reduction in the equilibrium yield of COCL2 favouring the original reactants CO + Cl2. (163)
This shows Le Chatelier’s principle as the system was able to neutralize the disturbance from its equilibrium.In this case, the change was the addition of molecules to the reactants. This caused an increase in the number effective collisions between the reactant’s molecules. Also, this raised the rate of the forward reaction. The system then has an increased amount of reactants and therefore has to travel in the forward direction to make extra products. This occurred in order to return the system to equilibrium by removing some of the excess reactants. By shifting in the forward direction, more products are being produced by the excess reactants. This ensures that the forward and reverse reaction rates are equal, which brings the system back to a state of
Data from previous studies suggest that the inactive sHSP takes on the oligomer conformation Upon stress, these oligomers assemble into active dimeric species, exposing previously inaccessible hydrophobic surfaces that can then interact with nonpolar patches on the misfolded substrate, capturing them in large complexes. The sHSP-substrate complexes maintain the substrate in a folding-competent state for extended periods of time. Biologically this is of utmost importance since it is
point at which the protein degrades and denatures – or falls apart into its lower levelstructures. Denatured proteins will often return to their original state, after the removal of the denaturing agent, except when they are degraded multiple levels (such as Quaternary to Secondary). Rate of reaction through catalysis can also be increased by increasing the concentration of either the enzyme or the reactants; enzyme if all the active sites are full or the substrate if the active sites are not all full.
is loss of its structure. This occurs when the ionics and hydrogens bonds of the protein
Hydrogen Bonds – These arise between the R-CO-R and the R-NH-R, and increase the boiling point of the structure of the enzyme as more energy is required to break the intermolecular bonds. This means that the enzyme can function at a higher than normal temperature.
In this experiment the process of osmosis is being observed and the different conditions in which osmosis occurs. In the egg osmosis experiment kinetic energy is used making this process a passive transport ‘in passive processes concentration or pressure differences drive the movement (Marieb,Smith, 2007)’ since ATP is not required which is called facilitated diffusion.
4.15. The purpose of this investigation was to use our knowledge on osmosis and diffusion and apply it to a de-shelled egg and see how it reacts being submerged in a sodium chloride solution. The hypothesis was that the egg would expand and increase in both size and weight this is proven correct in the table of
There are three factors that will alter an enzyme: temperature, pH and salt. All three will change the structure of the enzyme by denaturation and rendering it useless when a drastic change occurs from levels that are normal. A slight alteration can speed up reaction to certain saturation or slow the process of reaction.
Meanwhile, if temperature is increased denatures the proteins. Proteins then unfold and the non-polar groups which were previously in the interior of the molecule become exposed. This leads to a decrease in the solubility of the protein in aqueous environment. Addition of ethanol, methanol, acetone and the like decreases the dielectric constant and thus decreases protein’s solubility. (Boyer, 2000)