Hen Egg: The Best Source of Protein

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The ability to objectively understand the benefit of eggs, play a significant role in terms of identifying how eggs could be utilized as an important prerequisite for health. Eggs are made up of various nutrients which include vitamins, fat, mineral, and water, and could be an excellent source of dietary health. They are low in caloric intake typically around 75 cal primarily from frat and protein, a larger egg will contain up to seven grandes of protein, 4 g of fat, and 3 g that essentially come from the yolk. Eggs have historically been leveraged as an effective benchmark to ensure that there is consistency and quality of product and protein. This is caused the egg to be reference and benchmark is the primary source of protein, based upon its efficiency and ability to be healthy source of food (Brown, 2011).

To effectively understand the various components associated with an egg, one must have an objective appreciation of the structure. The five various structural components of an egg are the yolk, the egg white, the cell membrane, the air cell, and the shell. Each of the specific components plays a significant role in contributing to the various attributes and properties of eggs, which can assist in understanding their nutritional value. Yolk is representative of 30% of the egg, the egg white is representative of 50% of the a, and shell is representative of 12% of the egg mass. The eggs and the eggs whites are representative of a significant source of protein, and each of these has its own distinctive characteristics and properties.

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Being able to objectively understand the various components associated with an egg, is of the utmost importance. Over half of all the proteins in the egg are comprised of ovalbumin, which is necessary within the caloric intake. The Ovotransferrin (conalbumin) and Ovomucoid. Ovotransferrin, place if he can role in protecting against various forms of bacterial contamination by creating a complex interaction with the iron to protect against bacteria and ensure growth (Brown, 2011). These various forms of protein are resistant to the denaturation process which inhibits the activity of trypsin which is an effective enzyme that breaks down the protein. The Lysozyme was an additional type of enzyme that assist in fighting bacteria in protecting against viruses. The Avidin that is present in uncooked eggs binds with the B vitamin Biotene, which prevents it from being absorbed within the small intestine. This is why it is potentially dangerous to excessively consume raw egg whites, but when cooked it will no longer inhibit the absorption of biotin. A total 3 g of protein are found in the egg yolk which also plays a significant role in objectively understanding food preparation.

The ability to understand the thermal properties of hen egg protein, also plays a significant role in understanding the composition. The hen egg has several various functional properties which include foaming and emulsifying. This directly suggests that physicochemical and functional properties could be leveraged to create a transforming result within the application of various food products. It however is a challenge to separate the individual components of a Gill, but the implementation of a fractionated simple dilution and centrifugation, of the egg yolk can play significant role in enlarging the application thus increasing the value.

The implementation of Differential Scanning Calorimeter (DSC) or the potential implementation of a turbid metric method, provide three different peaks that include conalbumin, lysozyme (intermediate peak) and also the ovalbumin peak (Brown, 2011). There are also other proteins that are integrated within the egg white as these peaks have the capacity to vary in range based upon pH levels. With the implementation of an increase in denaturation temperature of the egg protein , the temperature of the egg white protein will inevitably start to increase. The understanding of the various thermal properties provides invaluable insight regarding interaction, and the precise ways the thermal and protein properties have the capacity to interact within this process.

Being able to understand the various biological activities derived within a components, can provide important health and nutritional information. Besides the protein that is widely known within eggs, there are several types of micronutrients within eggs that provide invaluable nutrition for the body. These micronutrients would include vitamin E, vitamin A, carotenoids, and selenium (Brown, 2011). These play a significant role and acting as a potential antioxidant, promoting health. Research found that three specific types of protein are manifested within the egg whites which include Ovalbumin, lysozyme and conalbumin.

Obalbumin carries the most abundant protein that is present within the egg white. Sodium Dodecyl Sulphate – Polyacrylmaide Gel Electrophoresis (SDS-PAGE) analysis has been used to reveal 14 major brands of egg protein, the differentiated based upon strategic variations of molecular weight. For example, Ovalbumin has various properties that include 385 amino acids while ovotransferrin is representative of 12 to 13% of the total egg white protein (Brown, 2011). Illustrative that was identified was Lysozyme which also contained a total of 18 amino acids, which also include binding agents such as glycation end products (Brown, 2011). This becomes a direct representation of the various protein structure and physiochemical based properites. This directly reinforced and solidified the goal of the research which was used to identify hen protein isoforms, to identify the various structural makeup.

The functional application of eggs within their various forms, make it a staple diet so having an objective understanding of the physiological makeup plays a significant role in promoting health. They are often combined with other ingredients, mixed with other types of foods, and used for various health purposes. They offer a specific ability to provide flavor, thicken, are used in bread, and various forms of baking, ensuring the eggs have functional application and diversification within products. Eggs also are implemented within various food purposes in preparation which would include processed meats, snacks, and entrées (Pszczola, 2006). This reinforces the understanding of these unique properties, because they play a significant role within food processing.

Egg white proteins have been utilized within various forms of cooking and ingredient processing. Ovalbumin for instance contains the vast majority of the egg white protein in terms of mass, with a weight of 44.5KDa and isoelectric point of 4.5 (Pszczola, 2006). This is also the only egg white protein which essentially contains free sulfhydryl groups representing over 385 residues. This also is representative as the bacteria inhibiting form derivative of egg whites, which contain 12% of the egg white protein which includes 686 amino acid residues and has 15 disulfide bridges (Davis, 2015). This has direct implications for the harvesting of eggs, as eggs that derive from younger flocks should remain any warmer temperature prior to being placed in a cooler environment. This will ensure that the proper development of various biological components within the egg white take place, and 12°C is representative of the optimum storage temperature to ensure proper maturation (Brake. et al, 1997). It is imperative that these optimal external factors are controlled, as they become a direct representation of the hatching success and the specific characteristics of albumen which are found within the egg.

Eggs also play a significant role in terms of understanding the various components of bioactivity compounds, and the precise ways that they are considered to be a functional food. The vast majority of eggs are considered to be bioactive components, which could be utilized for various human issues that affect human health. There has been research which has found excessive consumption of eggs could be associated with an increased probability for the development of type II diabetes, and potential cardiovascular and cholesterol issues (Davis, 2015). One large egg essentially contains 7 g of protein rich amino acid, and egg white protein has the ability to influence inflammation. Ovotransferrin is the primary component that has been shown to reduce inflammatory colitis pathology in a DSS-induced mouse model of colitis (Kobayashi Y, et. al 2015 This directly coincides with the structure of egg whites as the naturally exerts antimicrobial activity against Gram positive and Gram-negative bacteria through hydrolysis in the bacterial cell wall (Yokooji T, 2013).

This is directly representative of how eggs contain a very early variety of bioactive components which directly have the ability to reduce inflammatory processes within the body. The degree in which information is affected is contingent upon several factors which would include body weight, current health status, amount of consumption, and several other forms of health patterns (Tannock LR, et. al, 2005). This directly reinforces the evaluation of how an egg production has the capacity to influence the human body contingent upon consumption and different health risks.

The understanding of the protein extraction process also plays a significant role in understanding the precise ways the proteins could be used and extracted. Ovalbumin for instance is representative of extraction leveraging ammonium sulfate under acidic condition. Therefore, considering, as the use of ammonium sulfate was not satisfactory, the SDS-PAGE was used for a better result but the collected protein was denatured during the separation process (Yokooji T, 2013). This also reinforces the reason why , ion exchange chromatography has been the primary mechanism that has been utilized within a laboratory scale within egg white protein extraction, because of the low denaturation and release a non-altered by product. This method is also applicable on an industrial level, and is the most cost-efficient the could be utilized within industrial use. The recovery yield of ovotransferrin was estimated at 78% by HPLC analysis. The ovotransferrin fraction elution from the column was performed with a isocratic elution at 0.5M NaCl ((Brake. et al, 1997)

Hen egg allergies must be taken seriously, as they are representative of one of the primary sources of food poisoning for infant and young children. This is also considered one of the most commonly known food allergen components, and must be labeled within food packaging. The primary allergens that exist within a proteins are ovalbumin, ovalbumin, ovomucoid and lysozyme. The remaining protein content such as macroglobulin, avidine and several different enzymes is less significant (Sabine H. et al, 2008). The research suggests that the implementation of enzymatic hydrolysis of hen’s egg protein could could be utilized as an effective medium to reduce allergens and potential food problems. Heat treatment and purified egg protein could be used as an effective mechanism to reduce potential allergic reaction. Pasteurization can play a significant role in reducing the potential dangerous effects of allergens, as hen eggs are staple within diet so understand the potential risks is an area that is of the utmost importance.

The direct understanding of these various components plays a significant role in better utilizing hen eggs within society. The research clearly outlines the various benefits and protein benefits that this food source can offer, and its precise impact upon health. The paper also identify potential risk factors which would include the manifestation of the development of type II diabetes and cholesterol issues, and the importance of understanding how allergy control should be implemented. The strategic implementation of these various processes can ensure that the industry continues to progress, creating a safe food environment for all. By understanding the collective body of research, the various benefits associated with hen eggs can act as a strategic advantage which will ensure lasting sustainability within the food diet.

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