သၠာဲခၟာဲ

thumb|ခဍမ်ခၟာဲမွဲ ဂျိုင်င် မနွံလဒေါဝ် သၠာဲခၟာဲ
သၠာဲခၟာဲ (Egg white) ဂှ် ဒှ်ခၞတ်ကေဝ်ကေဝ် မနွံ အပ္ဍဲ ခၟာဲမွဲမရ။ ခၟာဲစာင်မ္ဂး နွံသဏ္ဌာန် လ္ပါ်ဂတဂှ် နွံဂၠိုင် ဟိုတ်နူကဵု ပ္ဍဲအခိင်စာင် မဂိုတ်ပ္တိတ်ခၟာဲဂှ်ရ။ သၠာဲခၟာဲဂှ် ပူဗိုင်လဝ် ခဍန်ခၟာဲရ။ ခဍန်ခၟာဲဂှ် နွံသန္ဓိကဵုဒှ် သက္ကုသန္ဓိကဵုဒှ် သၠာဲခၟာဲဂှ် ပူဗိုင်လဝ်ခဍန်ခၟာဲရ။ တင်ရန်တၟအ် အဓိကကမၠောန် သၠာဲခၟာဲဂှ် သွက်ဂွံ စဵုဒၞာ ခ္ဍန် ကေုာံ သွက်ဂွံဖ္ဍိုက်ဗပေင် အဟာရ ကုကောန်သန္ဓိ သွက်ခၟာဲသန္ဓိတအ်ရ။ 
သၠာဲခၟာဲဂှ် မတၟုဲတဴ ဗွဲမဂၠိုင် နကဵု ဍာ် ၜိုတ် ၉၀% သၟေဟ် ၁၀% ဂှ် ဒှ်ဓါတ် ပရဝ်တိန်ဂမၠိုင် (မပ္တံကဵု အလ်ဗူမိန် (albumins)၊ မုခဝ်ပရဝ်တိန် (mucoproteins)၊ ကေုာံ ဂလဝ်ဗူလိန် (globulins))တုဲ လေင်ဒၟံင်ရ။ သၠာဲခၟာဲဂှ် ဟွံတုပ် ညံင်ခဍန်ခၟာဲ၊ ခဍန်ခၟာဲဂှ် နွံကဵု ဓါတ်လဳပိဒ် (ကၠေင်) ဗွဲမဂၠိုင်တုဲ သၠာဲခၟာဲဂှ် ဓါတ်ကၠေင် ကြပ်ဟွံမဲတုဲ ဓါတ် ကာဗဝ်ဟာက်ဒြိတ် (carbohydrate) နွံ အောန်နူ ၁%ဏီရ။ ပ္ဍဲကဵု ခၟာဲမွဲမဂှ် ဓါတ်ပရဝ်တိန် နွံပ္ဍဲသၠာဲခၟာဲ ၜိုတ် ၅၆% ဒှ်ရ။ သၠာဲခၟာဲဂှ် စကာပ္ဍဲကဵု စၞစဂၠိုင်ကွေဟ်ရ။ ညံင်ရဴဂှ်ကီု ပ္ဍဲကာလမကၠောန် ဝက်သိန် (ဂဥုဲစဵုဒၞာ) လေဝ် စကာ သၠာဲခၟာဲ ဗွဲမဂၠိုင်ကီုရ။ ဗွဲတၟေင် ပ္ဍဲကာလမကၠောန် ဝက်သိန်ယဲချာမ်။).

လဒက်ပတန် 
ပ္ဍဲ သၠာဲခၟာဲစာင်မွဲမဂှ် ပထောအ် ပိဂအုမ်မ္ဂး သၠာဲဍေဟ် နွံလျိုင် ၜါဂအုမ်ဒှ်ရ။ ပ္ဍဲဂှ် ဍာ်နွံ ၉၀% သၟေဟ်ဂှ် ဒှ်ဓါတ်ပရဝ်တိန်၊ ဓါတ်သတ္တု၊ ဓါတ်ကၠေင်ဂမၠိုင်၊ ဝဳတမိန် ကေုာံ ဓါတ်ဂလူကောတ် တအ်ရ။ ခၟာဲစာင်အမေရိကာန်ဂျိုင်င် ဇၞော်မွဲမ မ္ဂး နွံသၠာဲ ၜိုတ် ၃၃ ဂရာမ်မ္ဂး၊ ပ္ဍဲဂှ် ၃,၆ ဂရာမ်ဂှ် ဒှ်ဓါတ်ပရဝ်တိန်၊ ၀,၂၄ ဂရာမ်ဂှ် ဒှ် ကာဗဝ်ဟာ်ဒြိတ် တုဲ ၅၅ မဳလဳဂရာမ် ဒှ်ဓါတ်သဝ်ဒဳယာမ် (sodium)။ ပ္ဍဲကဵုသၠာဲဂှ် ဓါတ်ခဝ်လေသ္ထရောလ် (cholesterol) တုဲပၠန် ဒြဟတ်ဂှ် နွံၜိုတ် ၁၇ ခလဝ်ရဳ (calories) သၠာဲခၟာဲဂှ် ဒှ်ဂကောံဓါတ်အလ်ကာလဳ (alkaline solution) တုဲ နွံကဵုဓါတ်ပရဝ်တိန် ၜိုတ် ၁၄၉ ဂကူရ။ သ္ၚိအင်သၟဝ်ဝွံ ဗၟံက်ထ္ၜးလဝ် ဂကူဓါတ်ပရဝ်တိန်ဂမၠိုင် မနွံဒၟံင် ပ္ဍဲသၠာဲခၟာဲဂမၠိုင် နကဵု တၟအ်ကၠံ ကေုာံ ယၟုဍေဟ်တအ်ရ။

Ovalbumin is the most abundant protein in albumen. Classed as phosphoglycoprotein, during storage, it converts into s-ovalbumin (5% at the time of laying) and can reach up to 80% after six months of cold storage. Ovalbumin in solution is heat-resistant. Denaturation temperature is around 84°C, but it can be easily denatured by physical stresses.
Conalbumin/ovotransferrin is a glycoprotein which has the capacity to bind the bi- and trivalent metal cations into a complex and is more heat sensitive than ovalbumin. At its isoelectric pH (6.5), it can bind two cations and assume a red or yellow color.  These metal complexes are more heat stable than the native state. Ovomucoid is the major allergen from egg white and is a heat-resistant glycoprotein found to be a trypsin inhibitor.  Lysozyme is a holoprotein which can lyse the wall of certain Gram-positive bacteria and is found at high levels in the chalaziferous layer and the chalazae which anchor the yolk towards the middle of the egg. Ovomucin is a glycoprotein which may contribute to the gel-like structure of thick albumen. The amount of ovomucin in the thick albumen is four times as great as in the thin albumen.

Foam 
thumb|Visual representation of protein denaturation. A globular protein becomes unfolded when exposed to heat. 
thumb|Aerated egg whites are frequently employed in shaken cocktail recipes, such as this Ramos gin fizz, for textural and aesthetic purposes.
The physical stress of beating egg whites can create a foam.  Two types of physical stress are caused by beating them with a whisk: denaturation and coagulation.

Denaturation occurs as the whisk drags the liquid through itself, creating a force that unfolds the protein molecules.

Coagulation comes from the mixing of air into the whites, which causes the proteins to come out of their natural state.  These denatured proteins gather together where the air and water meet and create multiple bonds with the other unraveled proteins, and thus become a foam, holding the incorporated air in place, because the proteins consist of amino acids; some are hydrophilic (attracted to water) and some are hydrophobic (repelled by water).

When beating egg whites, they are classified in three stages according to the peaks they form when the beater is lifted: soft, firm, and stiff peaks. Overbeaten eggs take on a dry appearance, and  eventually collapse. Egg whites do not beat up correctly if they are exposed to any form of fat, such as cooking oils or the fats contained in egg yolk.

Copper bowls have been used in France since the 18th century to stabilize egg foams. The copper in the bowl assists in creating a tighter bond in reactive sulfur items such as egg whites.  The bond created is so tight that the sulfurs are prevented from reacting with any other material.  A silver-plated bowl has the same result as the copper bowl, as will a pinch of powdered copper supplement from a health store used in a glass bowl.  Drawbacks of the copper bowl include the expense of the bowl itself, and that the bowls are difficult to keep clean.  Copper contamination from the bowl is minimal, as a cup of foam contains a tenth of a human's normal daily intake level.
thumb|Beaten egg whites

Health issues 
Although egg whites are prized as a source of low-fat, high-protein nutrition, a small number of people cannot eat them.  Egg allergy is more common among infants than adults, and most children will outgrow it by the age of five.  Allergic reactions against egg white are more common than reactions against egg yolks.  In addition to true allergic reactions, some people experience a food intolerance to egg whites.

Eggs are susceptible to Salmonella contamination. Thorough cooking eliminates the direct threat (i.e. cooked egg whites that are solid and not runny), but the threat of cross-contamination remains if people handle contaminated eggs and then touch other foods or items in the kitchen, thus spreading the bacteria. In August 2010, the FDA ordered the recall of 380 million eggs because of possible Salmonella contamination.

Cooked eggs are a good source of biotin. However, daily consumption of raw egg whites for several months may result in biotin deficiency, due to their avidin content, as the avidin tightly binds biotin and prevents its absorption.

Uses 
Egg white is a fining agent that can be used in the clarification and stabilization of wine. Egg white can also be added to shaken cocktails to create a delicate froth. Some protein powders also use egg whites as a primary source of protein.

The albumen from egg white was used as a binding agent in early photography during an 1855-90 period; such prints were called albumen prints.

In the 1750s, egg whites were believed to prevent swelling, and were used for that purpose. To help soothe areas of skin that were afflicted, egg white mixed with Armenic bole could help restore the fibers. Egg whites are also used in bookbinding during the gilding process, where it is referred to as 'glaire', and to give a book cover shine.

See also 

 Egg yolk
 Egg white substitutes
 Albumen print
 Haugh unit, a unit of measure for egg albumen
 Meringue, a dessert or dessert ingredient made from egg white
 Protein quality

References

Further reading 

 Gilbertus. Compendium Medicine Gilberti Anglici Tam Morborum Universalium Quam Particularium Nondum Medicis Sed & Cyrurgicis Utilissimum.  Lugduni: Impressum per Jacobum Sacconum, expensis Vincentii de Portonariis, 1510.
 Good Eats, Let Them Eat Foam. DVD. Television Food Network, June 13, 2001.

External links 

 Elmhurst College, Denaturation Protein
 Exploratorium, Anatomy of an Egg
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