Editing Casein (section)

===Food===
Several foods, creams, and toppings all contain a variety of caseinates. Sodium caseinate acts as a greater food additive for stabilizing processed foods; however, companies could opt to use [[calcium caseinate]] to increase calcium content and decrease sodium levels in their products.<ref name=":0">{{cite patent | inventor = Merrill RK, Li J | assign = Leprino Foods Co | title = Micellar casein for corree creamers and other dairy products. | country = US | number = 20160374360 | pubdate = 29 December 2016 | url = https://patents.google.com/patent/US20160374360A1/en }}</ref>

Caseins for food additive use are produced by adding an acid to milk, which causes the casein to precipitate out as ''acid casein''. By adding a base such as sodium hydroxide or calcium hydroxide to acid casein, a pure caseinate or ''casein salt'' is produced.<ref name="Badem">{{cite journal |last1=Badem |first1=A |last2=Ucar |first2=G |title=Production of caseins and their usages |journal=International Journal of Food Science and Nutrition |date=January 2017 |volume=2 |issue=1 |page=4-9 |url=https://www.researchgate.net/publication/330674713_Production_of_caseins_and_their_usages |issn=2455-4898}}</ref> "Co-precipate" refers to a mixture of casein and possibly other milk components that went out of the solution with casein. The precipitation can happen either through proteolysis (rennet) or through acid.<ref name="Badem"/>

{| class="wikitable"
|+Caseinate Presence and Function in Different Products<ref name=":1">{{Cite journal|vauthors=El-Bakry M|date=2011|title=Functional and Physicochemical Properties of Casein and its Use in Food and Non-Food Industrial Applications|journal=Chemical Physics Research Journal|volume=4|pages=125–138|id={{ProQuest|1707988596}}}}</ref>
!Product
!Caseinate %
!Type
!Function
|-
|Cheese
|3–28
|Rennet (digested) casein, some products also add [[milk protein concentrate]]<ref name="Badem"/>
|Matrix formation, fat, and water binding
|-
|Ice Cream
|1–7
|Calcium caseinate from milk, added caseinate
|Texture and stabilizer
|-
|Whipped toppings
|2–11
|Added caseinate
|Fat stabilization
|-
|Meat
|2–20
|Added caseinate and co-precipate
|Texture and nutrition
|-
|Pasta
|2–18
|Added caseinate and caseins
|Texture, nutrition, and taste
|-
|Baked goods
|1–15
|Added caseinate and caseins
|Water binding
|}
The main food uses of casein are for powders requiring rapid dispersion into water, ranging from coffee creamers to instant cream soups. Mead Johnson introduced a product in the early 1920s named Casec to ease gastrointestinal disorders and infant digestive problems which were a common cause of death in children at that time.

All caseinates have very efficient emulsifying properties and widely used to make emulsions in foods.<ref>{{Cite journal | vauthors = Courthaudon JL, Girardet JM, Campagne S, Rouhier LM, Campagna S, Linden G, Lorient D |date= March 1999 |title=Surface active and emulsifying properties of casein micelles compared to those of sodium caseinate  |journal=International Dairy Journal |volume=9 |issue=3 |pages=411–412 |doi=10.1016/S0958-6946(99)00111-9 |issn=0958-6946}}</ref><ref name="Braun_2019" />

Casein is also believed to neutralize [[capsaicin]], the active spicy ingredient of [[chili pepper]]s such as [[jalapeño]]s, and [[habanero]]s.<ref>{{cite journal | vauthors = Nolden AA, Lenart G, Hayes JE | title = Putting out the fire - Efficacy of common beverages in reducing oral burn from capsaicin | journal = Physiology & Behavior | volume = 208 | pages = 112557 | date = September 2019 | pmid = 31121171 | pmc = 6620146 | doi = 10.1016/j.physbeh.2019.05.018 }}</ref> Milk is often consumed to decrease irritation caused by spicy foods.

====Cheesemaking====
[[File:Production of cheese 1.jpg|thumb|left|Cheesemaking]]
[[Cheese]] consists of proteins and fat from [[milk]], usually the milk of [[Cow milk|cows]], [[Water Buffalo|buffalo]], [[Goat milk|goats]], or [[Sheep milk|sheep]]. It is produced by [[coagulation (milk)|coagulation]] that is caused by destabilization of the casein micelle, which begins the processes of fractionation and selective concentration.<ref name=wiley2002 /> Typically, the milk is acidified and then coagulated by the addition of [[rennet]], containing a [[proteolytic]] [[enzyme]] known as [[Chymosin|rennin]]; traditionally obtained from the stomachs of [[calf (animal)|calves]], but currently produced more often from genetically modified microorganisms. The solids are then separated and pressed into final form.<ref>{{cite web|url=http://biology.clc.uc.edu/fankhauser/Cheese/CHEESE.HTML|title=Fankhauser's Cheese Page| vauthors = Fankhauser DB |date=2007 |archive-url=https://web.archive.org/web/20070925001225/http://biology.clc.uc.edu/Fankhauser/Cheese/CHEESE.HTML|archive-date=25 September 2007|url-status=dead|access-date=23 Sep 2007}}</ref>

Unlike many proteins, casein is not coagulated by heat.  During the process of clotting, milk-clotting [[proteases]] act on the soluble portion of the caseins, [[K-casein|κ-casein]], thus originating an unstable [[micelle|micellar]] state that results in clot formation. When coagulated with [[chymosin]], casein is sometimes called '''paracasein'''. Chymosin (EC 3.4.23.4) is an [[aspartic protease]] that specifically [[hydrolysis|hydrolyzes]] the peptide bond in Phe105-Met106 of κ-casein, and is considered to be the most efficient protease for the cheese-making industry (Rao et al., 1998). British terminology, on the other hand, uses the term caseinogen for the uncoagulated protein and casein for the coagulated [[protein]]. As it exists in milk, it is a [[salt (chemistry)|salt]] of [[calcium]].

====Protein supplements====
An attractive property of the casein molecule is its ability to form a gel or clot in the stomach, which makes it very efficient in nutrient supply. The clot is able to provide a sustained slow release of amino acids into the blood stream, sometimes lasting for several hours. This also happens when milk is consumed by an animal: the stomach proteases cause it to form a gel. Cheesemaking using [[rennet]] (see above) replicates this behavior.<ref>{{cite journal | vauthors = Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrère B | title = Slow and fast dietary proteins differently modulate postprandial protein accretion | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 26 | pages = 14930–14935 | date = December 1997 | pmid = 9405716 | pmc = 25140 | doi = 10.1073/pnas.94.26.14930 | doi-access = free | bibcode = 1997PNAS...9414930B }}</ref>

Casein is also a relatively abundant source of protein. One form (without the delayed-gelling property) is ''hydrolyzed casein'', whereby it is [[hydrolysis|hydrolyzed]] by a [[protease]] such as [[trypsin]]. This could result in quicker digestion or direct gel formation. Hydrolyzed forms are noted to taste bitter and such supplements are often refused by infants and lab animals in favor of intact casein.<ref>{{cite journal | vauthors = Field KL, Kimball BA, Mennella JA, Beauchamp GK, Bachmanov AA | title = Avoidance of hydrolyzed casein by mice | journal = Physiology & Behavior | volume = 93 | issue = 1–2 | pages = 189–199 | date = January 2008 | pmid = 17900635 | pmc = 2254509 | doi = 10.1016/j.physbeh.2007.08.010 }}</ref>