This increases the smoothness and creaminess. Dispersion forces. Given that it would be very difficult to explain this phenomenon at the molecular level using the whole protein structure, my student uses chains of cysteine molecules linked by sulfur bonds as a model for egg white. to make a gravadlax or ceviche) is an example of protein acid denaturation. Therefore, the bonding disrupts faster and the rate of denaturation increased. The unfavourable interactions produced between protein molecules leaded to the connection of protein molecules. The primary structure consists of the specific amino acid sequence. Furthermore, the sample of yoghurt with fresh milk was detected a tangier taste in comparison with the sample with boiled milk and the original sample. Denaturation processes of egg protein cause the breaking of hydrogen bonds, holding them together, and also disrupts the peptide bonds holding the structure of individual proteins. If you overwhip them then you completely denature them and form clumps of tangles

Acid will help in denaturing the protein. Egg yolks also contain significant amount of protein (52% water, 16% protein by mass), but also significant amounts of lipids (27% lipids by mass). Since then, a proportion of milk is taken to fluid called whey. This will cause molecules to vibrate quickly and this breaks the bonds, causing the protein structure to unravel. Since then, there was a chance for long chain of polypeptides to interact with other polypeptides and the polypeptides were reformed to large molecular structure to form coagulum. The denaturation of the proteins of egg white by heatas when boiling an eggis an example of irreversible denaturation. When the water is boiling put 1 cup . Eggs are mostly albumen, milk is largely casein . At acid pH (pH 3.0 . These molecules, because of their high affinity for peptide bonds, break the hydrogen bonds and the salt bridges between positive and negative side chains, thereby abolishing the tertiary structure of the peptide chain. But highly organized structures tend to have a certain delicacy, and this is true of proteins. When a protein denatures, its complicated folded structure unravels, and it becomes just a long strand of amino acids . Spoon, Fork Alcohol Vinegar Water Glass containers/Medicine Cups (5) Stove Frying Pan Spatula Syringe (for measuring volume) Tissue Procedure: Preparation of Egg Albumin Solution Add 5 mL of. Denaturation does not involve identical changes in protein molecules. These compounds are capable of engaging in intermolecular hydrogen bonding with protein molecules, disrupting intramolecular hydrogen bonding within the protein. There are more than 40 different proteins in a whole egg, some only located in the white and others predominantly in the yolk. It is believed that the organic solvents interfere with the mutual attraction of nonpolar groups. Legal. Protein Sci. When a protein is denatured the overall shape . The proteins in the egg white are more sensitive to heat than those in the egg yolk. of clear 1% egg white solution, add 2ml of hydrochloric acid. Registered office: Creative Tower, Fujairah, PO Box 4422, UAE. Four major types of attractive interactions determine the shape and stability of the folded protein: ionic bonding, hydrogen bonding, disulfide linkages, and dispersion forces. Add 6M HCl dropwise into the eggwhite. This helix is stabilized by intrachain hydrogen bonding between the carbonyl oxygen atom of one amino acid and the amide hydrogen atom four amino acids up the chain (located on the next turn of the helix) and is known as a right-handed -helix. Learn the causes behind this occurrence by understanding the four levels of protein structure: Primary, secondary, tertiary, and quaternary. Two samples of yoghurt with respective addition of fresh milk and boiled milk cultured in 38 incubator formed two layers: firm and thickened milky gel and yellow watery surface. These segments of secondary structure are incorporated into the tertiary structure of the folded polypeptide chain. The egg white should be in a glass container as to not risk unfavorable reactions between strong acids and some plastics. Update your browser to view this website correctly. Interesting among denaturing agents are those that affect the secondary and tertiary structure without affecting the primary structure. In general, fairly vigorous conditions are needed to hydrolyze peptide bonds. The clear egg white turns opaque as the albumin denatures and coagulates. For example, the mutual attraction between an aspartic acid carboxylate ion and a lysine ammonium ion helps to maintain a particular folded area of a protein (part (a) of Figure \(\PageIndex{5}\)). Copyright 2023, The Rockefeller University. Add 3 l (or a single drop from a Pasteur pipette) 0.5 M HCl to each sample and observe. The final conformation is probably frozen when the peptide chain attains a length of 50 or more amino acid residues. The time duration for baking at around 130 in the oven was 30 minutes in order to make egg custard. Dispersion forces are weak but can be important when other types of interactions are either missing or minimal (part (d) of Figure \(\PageIndex{5}\)). Such evidence suggests that, at least for these proteins, the primary structure determines the secondary and tertiary structure. Disclaimer: This is an example of a student written essay.Click here for sample essays written by our professional writers. Explore Place an egg white into a clean bowl Observe the colour and texture of the egg white Now add 3ml of lemon juice to the egg white and stir Record what happens to the colour and texture of the egg white Egg white turns solid and goes white instead of clear when it denatures Meat and Education.com worksheet: What makes meat tender The egg is used in the preparation of many confectionary items such as cakes, this is used because, when the denaturation of the egg protein occurs, it has the property of binding different substances. The first of these is the primary structure, which is the number and sequence of amino acids in a proteins polypeptide chain or chains, beginning with the free amino group and maintained by the peptide bonds connecting each amino acid to the next. So the acid helps the denaturing process rather than provides bonds in the new foam. On comparing the two processes that can most commonly disrupt the egg proteins, it was found that the heat could denature the proteins and cause the hardening of egg and yolk in 8-10 minutes while the alcohol takes a comparatively longer time to do so. In these proteins, the chains are folded so that the molecule as a whole is roughly spherical. Any or all? coagulation due to evaporation of water molecules from denaturation of egg protein (Chandra et . Chemically, this is the process by which the chains of amino acids are changed from their original (or native) state. Moreover, a gel-like structure was formed. 2.3: Denaturation of proteins is shared under a CC BY-NC-SA 4.0 license and was authored, remixed, and/or curated by LibreTexts. The denaturation of the proteins of egg white by heatas when boiling an eggis an example of irreversible denaturation. On the chemistry front a few questions myself. Free resources to assist you with your university studies! Depending on the nature of the side chains, this may result in the formation of an -helix or of loops closed by hydrogen bonds or disulfide bridges. Some salts, such as ammonium sulfate, tend to stabilize protein . Denaturation is the term used for any change in the three-dimensional structure of a protein that renders it incapable of performing its assigned function. Subsequent oxidation and linkage of the sulfur atoms in the highly reactive sulfhydryl (SH) groups leads to the formation of cystine (part (c) of Figure \(\PageIndex{5}\)). Feel free to use whatever terminology you're familiar with - if it exceeds my level of understanding I'll do some research myself to figure out what you're saying. The time durations for changes in the three tubes were 1 minutes 22 seconds, 19 minutes and 20 minutes respectively. Stirring Rods Graduated cylinder. Protein denaturation When a solution of a protein is boiled, the protein frequently becomes insolublei.e., it is denaturedand remains insoluble even when the solution is cooled. Although denaturation had long been considered an all-or-none reaction, it is now thought that many intermediary states exist between native and denatured protein. The heat from a pan denatures the albumin protein in the liquid egg white and it becomes insoluble. The eggs are an important source of proteins. A wide variety of reagents and conditions can cause a protein to unfold or denature. No one has yet reversed that process. (You can visit USDAs National Nutrition Database for more details.). The arrangement of multiple subunits represents a fourth level of structure, the quaternary structure of a protein. Thus, the mixture became semi-solid phase or a gel-like structure. Overall an egg is just under 13% protein by mass. By contrast, water and water soluble substances had smaller molecular structure and lighter mass. Swirl slightly to observe the chemical changes happening over time. Unfortunately, she's hit a roadblock when it comes to explaining the chemical reactions that cause this, and her teacher is being very cryptic about the whole thing.

Egg white consists mainly of water and protein, with carbohydrates and minerals added to the mix. When denaturing agents are removed from a protein solution, the native protein re-forms in many cases. 2. All rights reserved. Please allow a few moments for large files to process. nitric acid in a test tube (CAUTION!). Milk protein had large molecular structure and heavier mass. Denaturation refers to the physical changes that take place in a protein exposed to abnormal conditions in the environment. The structure of proteins is generally described as having four organizational levels. Eggs are high in protein, therefore these are healthier muscles, bones, and hair. Hair and the outer layer of skin are composed of keratin. We've received widespread press coverage since 2003, Your UKEssays purchase is secure and we're rated 4.4/5 on reviews.co.uk. However, there was no observable change in egg white solution with additions of equal of volume of distilled water. Describe the four levels of protein structure. A schematic representation of the four levels of protein structure is in Figure \(\PageIndex{7}\). Hemoglobin, with four polypeptide chains or subunits, is the most frequently cited example of a protein having quaternary structure (Figure \(\PageIndex{6}\)). (It will be useful to draw out the chromosomes of each fly and follow the alleles throughout the cross.) Cooks have taken advantage of this for many years. For a better experience, please enable JavaScript in your browser before proceeding. Cysteine does play a role with sulfur bonds in stabilizing the whipped eggs but most of the stabilization is simple denaturing. [Pg.185] In this experiment, you will determine the temperature that will denature proteins like albumen, casein, and keratin. Heat, acid, high salt concentrations, alcohol, and mechanical agitation can cause proteins to denature. What is Denaturation Of Proteins: Agents of Denaturation & Affect of Denaturation on Proteins. When a solution of a protein is boiled, the protein frequently becomes insolublei.e., it is denaturedand remains insoluble even when the solution is cooled. The denatured protein has the same primary structure as the original, or native, protein. The protein gets denatured due to the effect of higher temperature. We think of cooking using heat; however, the proteins can also be denatured with a strong acid to disrupt the intermolecular forces chemically. Egg whites. Describe acid as a What to learn next based on college curriculum. If passing the sample around to students, ensure the sample is securely closed or that students are also wearing personal protective equipment. What are the effects of denaturation? Some proteins, such as gamma globulin, chymotrypsin, and cytochrome c, have little or no helical structure. At the secondary through quaternary levels, however, proteins are quite vulnerable to attack, though they vary in their vulnerability to denaturation. A common property of denatured proteins, however, is the loss of biological activitye.g., the ability to act as enzymes or hormones. What Is the Difference Between a Peptide and a Protein. Denaturation is the phenomenon or process through which the proteins become unstable as their structure is being disrupted through various agents such as cooking or using alcohol. 2.5: Denaturation of proteins is shared under a CC BY-NC-SA 4.0 license and was authored, remixed, and/or curated by LibreTexts. The isoelectric point of ovalbumin and conalbumin (~79% of the proteins in egg white altogether) are at pH 4.6-4.8 for ovalbumin, and 5.6-6.0 for conalbumin. . The original sample of yoghurt was light, fluffy, smooth and creamy and tasted a bit sour and the smell of milk was detected. This leads to the disruption of bonds holding the protein together. Connective tissues contain collagen. This leads to the denaturation of the protein. Proteins in things lik. A wide variety of reagents and conditions can cause a protein to unfold or denature. Is it forming bonds or IMFs? [ 1 ]In the practical, the denaturation of egg white and milk were examined. The decrease of lysine was higher in the cooked chickpea seeds than in the heated protein fractions, globulins and albumins. Before the treatment of different conditions, the milk was white liquid in each of three tubes and the conical flask. I don't understand what you're asking.

You want to know why acid is making the egg white become stable and firm? The measurement of milk in pHjwas 6.39. Finally, the conical flask sample was taken for centrifugation for 5 minutes at 2,000rpm. Figure \(\PageIndex{4}\) shows a depiction of the three-dimensional structure of insulin. The -keratins, found in hair and wool, are exclusively -helical in conformation. The reason was that the higher the temperature of the water bath, the more the heat energy was supplied to protein molecules per unit time. HCl 1% AgNO3 Ethanol. Another common type of secondary structure, called the -pleated sheet conformation, is a sheetlike arrangement in which two or more extended polypeptide chains (or separate regions on the same chain) are aligned side by side. { "2.1:_The_Structure_of_Proteins" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "2.2:_Protein_Folding" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "2.3:_Denaturation_of_proteins" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "2.4:_Amino_Acids_and_Proteins_(Exercises)" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()" }, { "01:_Amino_Acids" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "02:__Protein_Structure" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "03:_Methods_of_Protein_Purification_and_Characterization" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "04:_Overview_of_Hemoglobin_and_Myoglobin" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "05:_Michaelis-Menten_Enzyme_Kinetics" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "06:_Catalytic_Strategies_of_Enzymes" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "07:__Enzyme_Active_Site_and_Substrate_Specificity" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "08:_Enzyme_Regulation" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "09:_Carbohydrates" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "10:_The_Generation_of_Energy_from_Carbohydrate_Metabolism" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "12:_Oxidation" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()", "13:_The_Flow_of_Genetic_Information" : "property get [Map MindTouch.Deki.Logic.ExtensionProcessorQueryProvider+<>c__DisplayClass228_0.b__1]()" }, [ "article:topic", "Denaturation", "Renaturation", "showtoc:yes", "license:ccbyncsa", "transcluded:yes", "source-chem-16019", "licenseversion:40" ], https://chem.libretexts.org/@app/auth/3/login?returnto=https%3A%2F%2Fchem.libretexts.org%2FCourses%2FUniversity_of_Arkansas_Little_Rock%2FChem_4320%2FChem_4320%252F%252F5320%253A_Biochemistry_1%2F02%253A__Protein_Structure%2F2.3%253A_Denaturation_of_proteins, \( \newcommand{\vecs}[1]{\overset { \scriptstyle \rightharpoonup} {\mathbf{#1}}}\) \( \newcommand{\vecd}[1]{\overset{-\!-\!\rightharpoonup}{\vphantom{a}\smash{#1}}} \)\(\newcommand{\id}{\mathrm{id}}\) \( \newcommand{\Span}{\mathrm{span}}\) \( \newcommand{\kernel}{\mathrm{null}\,}\) \( \newcommand{\range}{\mathrm{range}\,}\) \( \newcommand{\RealPart}{\mathrm{Re}}\) \( \newcommand{\ImaginaryPart}{\mathrm{Im}}\) \( \newcommand{\Argument}{\mathrm{Arg}}\) \( \newcommand{\norm}[1]{\| #1 \|}\) \( \newcommand{\inner}[2]{\langle #1, #2 \rangle}\) \( \newcommand{\Span}{\mathrm{span}}\) \(\newcommand{\id}{\mathrm{id}}\) \( \newcommand{\Span}{\mathrm{span}}\) \( \newcommand{\kernel}{\mathrm{null}\,}\) \( \newcommand{\range}{\mathrm{range}\,}\) \( \newcommand{\RealPart}{\mathrm{Re}}\) \( \newcommand{\ImaginaryPart}{\mathrm{Im}}\) \( \newcommand{\Argument}{\mathrm{Arg}}\) \( \newcommand{\norm}[1]{\| #1 \|}\) \( \newcommand{\inner}[2]{\langle #1, #2 \rangle}\) \( \newcommand{\Span}{\mathrm{span}}\)\(\newcommand{\AA}{\unicode[.8,0]{x212B}}\), 2.4: Amino Acids and Proteins (Exercises), status page at https://status.libretexts.org, Heat above 50C or ultraviolet (UV) radiation, Use of organic compounds, such as ethyl alcohol. A protein may have up to four levels of structure. After the baking for 30 minutes, the mixture became thickened and semi-solid phase. The resulting peptide chain can form an -helix or -pleated sheet (or local structures not as easily categorized), which is known as secondary structure. The primary structure consists of the specific amino acid sequence. In each of 2 test tubes containing 3 ml. This gives the protein its shape. This can be done by addition of acids/bases to a protein. The quaternary structure describes the arrangements of subunits in a protein that contains more than one subunit. Besides, the time duration for change to occur at 80 was much shorter than that at 60. They may also be unstabilized by various agents such as alcohol and baking soda, which interfere in their structure by breaking the bonds attaching them. However, given the proper circumstances and enough time, a protein that has unfolded under sufficiently gentle conditions can refold and may again exhibit biological activity (Figure ). Accessibility StatementFor more information contact us atinfo@libretexts.orgor check out our status page at https://status.libretexts.org. A protein may have up to four levels of structure. Because there's plenty of information on that all over the internet.

There's also quite a lot of information available on the internet about how egg whites work, specifically. Denaturing a protein is occasionally irreversible (Top) The protein albumin in raw and cooked egg white. A protein molecule is not a random tangle of polypeptide chains. Egg white turns solid and goes white instead of clear when it denatures, Meat and Education.com worksheet: What makes meat tender, Meat and Education.com teachers' notes: What happens when meat is cooked, OCR topic exploration pack: Preparation techniques, 2017 The Institute of Food Science & Technology. Disan is a scientist and educator striving to share her curiosity and love of science with others. These proteins influence the rate of denaturation and coagulation. If a lot is around, then there will be a lot more cross links between those proteins. Denaturation refers to the physical changes that take place in a protein exposed to abnormal conditions in the environment. The protein in meat also denatures and becomes firm when cooked. http://www.milk.co.uk/page.aspx?intPageID=81, http://www.hsph.harvard.edu/nutritionsource/what-should-you-eat/protein/, http://www.ukessays.com/essays/biology/denaturation-of-egg-white-data-biology-essay.php, Examine and explain the changes in appearance of egg white that occur in different conditions in denaturation of egg white, Examine the phase transitions that occur in denaturation of egg and milk affected by temperature change by making egg custard, Examine and explain the changes in appearance of milk that occur in different conditions in denaturation of milk, Examine and explain the changes and differences in properties between the original sample of yoghurt and two sample with respective addition of fresh milk and boiled milk. At the same time, boiling or cooking the egg, the white part, which has a clear appearance, changes, and turns white. The delicately folded globular proteins are much easier to denature than are the tough, fibrous proteins of hair and skin. What is denaturation of protein give an example? Eggs: Egg whites are largely composed of albumin (protein) in water. Begin with 3.0 g egg white in a small glass container; ideally one with a lid for safe observation by students. The amount of lactose-consuming bacteria in sample of yoghurt with fresh milk was much higher than that with boiled milk. It was because the fresh milk did not involve a process of boiling that killed bacteria at boiling temperature. Procedure for Egg Albumin Denaturation: Denaturation by Heat 1. The white of an egg is a solution of protein in water which depends upon stable interactions with the protein active groups. 308 qualified specialists online. The tertiary structure is intimately tied to the proper biochemical functioning of the protein. I mean, the acid is denaturing the proteins (which is irreversible in the case of egg white). The acid is affecting the proteins in the egg white. These reagents combine with positively charged amino groups in proteins to disrupt ionic bonds. As proteins deform or unravel parts of structure that were hidden away get exposed and form bonds with other protein molecules, so they coagulate (stick together) and become insoluble in water. Alcohol. High amount of bacteria produced excessive lactic acid. There was a difference between the milk conditions because of different mass of substances. Denaturation can be caused by heat, acid or base exposure, or even violent physical action. The time required to achieve a particular degree of denaturation is inversely proportional to the rate constant for the process. Each of the thousands of naturally occurring proteins has its own characteristic amino acid composition and sequence that result in a unique three-dimensional shape. Instead, the chains are arranged in unique but specific conformations. Meanwhile, the water was trapped into the network of polypeptides. In the practical, the denaturation of egg white and milk were examined. This experiment can be done with acids of varying concentration, including distilled white vinegar that you probably have in your kitchen. The denaturation of many proteins, such as egg white, is irreversible. Abstract The paper deals with the influence of high pressure treatment of fresh egg white on its properties and protein composition (individual amino-acids predicted as a function of pressure and time levels). So would a base - see if she can get the eggs to whip more easily with baking soda or potassium hydroxide. Anyone who has fried an egg has observed denaturation. . An example of denaturation is the hardening of an egg white when the egg is boiled or fried. Two sample of yoghurt formed firm and thickened milky curd. A native protein has a complex, rigid structure and is functionally active. A student I tutor is working on a project that focuses on the chemistry of cooking. The aligned segments can run either parallel or antiparallelthat is, the N-terminals can face in the same direction on adjacent chains or in different directionsand are connected by interchain hydrogen bonding (Figure \(\PageIndex{3}\)). Ionic bonds result from electrostatic attractions between positively and negatively charged side chains of amino acids. The albumin protein in egg white is denatured by heating so that it forms a semisolid mass. The discovery of beaten egg white as a baking agent is a development of Renaissance cuisine in Europe. If an egg is kept in alcohol for a while, then the alcohol molecules attach to the bond of egg protein and start disrupting it, which is why it is also known as a "bond disruptor.". Sourness was enhanced in the sample of yoghurt with fresh milk. Proteins can be divided into two categories: fibrous, which tend to be insoluble in water, and globular, which are more soluble in water. Proteins are compounds of high molar mass consisting largely or entirely of chains of amino acids. 2. Prepare a same volume with double-distilled water as control. The white of an egg is a solution of protein in water which depends upon stable interactions with the protein active groups. Heat: Increased temperatures cause kinetic energy to increase as well. Result: The egg white protein becomes firm when heated. The condition. Like other proteins, egg proteins are also heated labile and get denatured if exposed to high heat. Serum albumin plays a major role in transporting fatty acids and maintaining a proper balance of osmotic pressures in the body. Eggs are a nutritious source of protein. of egg albumin solution with q ml. Visit RockEDU Programs at the Rockefeller University, Learn about the Styles of Scientific Reasoning, Review of Bonding and Intermolecular Forces, Thin Layer Chromatography (TLC) for the Separation of Lipids, Single Step Lipid Extraction From Food Stuffs, Glass petri dish, beaker, or jar (glass is best when working with strong acids), Micropipette and Micropipette Tips (if you do not have access to a micropipette, you can use a glass Pasteur pipette with a rubber bulb). The primary structures of proteins are quite sturdy. Changes in salt concentration may also denature proteins, but these effects depend on several factors including the identity of the salt. When the proteins are denatured, their chemical and physical properties change. It is an acidic salt because the acid dissociation constant (Ka) of the silver ion is significantly larger than the base dissociation constant of the nitrate ion. Begin with 3.0 g egg white in a small glass container; ideally one with a lid for safe observation by students. Curing salmon using lemon and lime juice (eg. Denaturation of egg protein takes place when the applied temperature is of a higher degree. Answer: Silver nitrate is what is known as an "acidic salt". Dilute 1 ml. denaturation, in biology, process modifying the molecular structure of a protein. The acid catalyzes the whole process, denaturing the proteins more quickly.

Proteins can and do denature on their own, but do it at a lower rate during egg white beating. The addition of heat or a decrease of pH are methods of denaturing or changing the nature of the protein. Proteins are the molecules that are heat-labile and undergoes a structure destabilization on being heated. A given sequence of amino acids seems to adopt its particular three-dimensional (3D) arrangement naturally if conditions are right. Proteins are denatured by treatment with alkaline or acid, oxidizing or reducing agents, and certain organic solvents. Ionic bonding. [2] When casein micelles were destabilized by acidic environment, due to denaturation, micelles stuck together. PROTEIN DENATURATION HEAT, ACIDS, SALTS, ACETONE CEEA Erasmus 7.36K subscribers Subscribe 176 32K views 5 years ago Soluble proteins from egg white are treated with different chemicals and. After the treatment of different conditions, the egg white in tubes made changes in appearance at certain time in water bath or at certain number of additions shown in the table. Salts of heavy metal ions, such as mercury, silver, and lead. Denaturation involves the breaking of many of the weak linkages, or bonds ( e.g., hydrogen bonds), within a protein molecule that are responsible for the highly ordered structure of the protein in its natural (native) state. Cooking an egg (or many other protein-rich foods) largely involves denaturing the proteins, and cross-linking them with each other to form the rubbery, white substance we are familiar with eating.