Gelatin - Wikipedia, The Free Encyclopedia
Content
05/01/2015
Gelatin Wikipedia, the free encyclopedia
Gelatin
From Wikipedia, the free encyclopedia
Gelatin or gelatine (from Latin: gelatus meaning "stiff",
"frozen") is a translucent, colourless, brittle (when dry),
flavourless foodstuff, derived from collagen obtained from
various animal byproducts. It is commonly used as a gelling
agent in food, pharmaceuticals, photography, and cosmetic
manufacturing. Substances containing gelatin or functioning in a
similar way are called gelatinous. Gelatin is an irreversibly
hydrolyzed form of collagen. It is found in most gummy candy as
well as other products such as marshmallows, gelatin dessert, and
some ice cream, dip and yogurt. Household gelatin comes in the
form of sheets, granules, or powder. Instant types can be added to
the food as they are; others need to be soaked in water
beforehand.
'Sheet' or 'leaf' gelatin for cooking
Contents
1 Composition and properties
2 Production
2.1 Pretreatments
2.2 Extraction
2.3 Recovery
3 Uses
3.1 Culinary uses
3.2 Technical uses
3.3 Other uses
4 Dietary restrictions and gelatin substitutes
5 Medical and nutritional properties
6 Safety concerns
7 References
Composition and properties
Gelatin is a mixture of peptides and proteins produced by partial hydrolysis of collagen extracted from
the skin, bones, and connective tissues of animals such as domesticated cattle, chicken, pigs, and fish.
During hydrolysis, the natural molecular bonds between individual collagen strands are broken down
into a form that rearranges more easily. Its chemical composition is, in many respects, closely similar to
that of its parent collagen.[1] Photographic and pharmaceutical grades of gelatin are generally sourced
from beef bones.
http://en.wikipedia.org/wiki/Gelatin
1/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
Gelatin forms a viscous solution when dissolved in hot water, which sets to a gel on cooling. Gelatin
added directly to cold water does not dissolve well. Gelatin is also soluble in most polar solvents.
Gelatin solutions show viscoelastic flow and streaming birefringence. The solubility of the gelatin is
determined by the method of manufacture. Typically, gelatin can be dispersed in a relatively
concentrated acid. Such dispersions are stable for 10–15 days with little or no chemical changes and are
suitable for coating purposes or for extrusion into a precipitating bath.
The mechanical properties of gelatin gels are very sensitive to temperature variations, the previous
thermal history of the gel, and time. These gels exist over only a small temperature range, the upper limit
being the melting point of the gel, which depends on gelatin grade and concentration (but is typically
less than 35 °C) and the lower limit the freezing point at which ice crystallizes. The upper melting point
is below human body temperature, a factor which is important for mouthfeel of foods produced with
gelatin.[2] The viscosity of the gelatin/water mixture is greatest when the gelatin concentration is high
and the mixture is kept cool (≈ 4 °C). The gel strength is quantified using the Bloom test.
Production
The worldwide production amount of gelatin is about
375,000 metric tons per year (roughly 827 million lb). On
a commercial scale, gelatin is made from byproducts of
the meat and leather industry. Recently, fish byproducts
have also been considered because they eliminate some
of the religious obstacles surrounding gelatin
consumption.[2] Gelatin is derived from pork skins, pork,
horses, and cattle bones, or split cattle hides.[3] The raw
materials are prepared by different curing, acid, and
alkali processes which are employed to extract the dried
collagen hydrolysate. These processes[4] may take up to
several weeks, and differences in such processes have
great effects on the properties of the final gelatin
products.[5]
Gelatin can also be prepared in the home. Boiling
certain cartilaginous cuts of meat or bones will
result in gelatin being dissolved into the water.
Depending on the concentration, the resulting
stock (when cooled) will naturally form a jelly or
gel. This process is used for aspic.
While there are many processes whereby collagen
can be converted to gelatin, they all have several
factors in common. The intermolecular and
intramolecular bonds which stabilize insoluble
collagen rendering it insoluble must be broken,
and the hydrogen bonds which stabilize the
collagen helix must also be broken.[1] The
manufacturing processes of gelatin consists of three main stages:
1. Pretreatments to make the raw materials ready for the main extraction step and to remove
http://en.wikipedia.org/wiki/Gelatin
2/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
impurities which may have negative effects on physio chemical properties of the final gelatin
product,
2. The main extraction step, which is usually done with hot water or dilute acid solutions as a multi
stage extraction to hydrolyze collagen into gelatin, and finally,
3. The refining and recovering treatments including filtration, clarification, evaporation, sterilization,
drying, rutting, grinding, and sifting to remove the water from the gelatin solution, to blend the
gelatin extracted, and to obtain dried, blended and ground final product.
Pretreatments
If the raw material used in the production of the gelatin is derived from bones, dilute acid solutions are
used to remove calcium and other salts. Hot water or several solvents may be used in order to reduce the
fat content, which should not exceed 1% before the main extraction step. If the raw material consists of
hides and skin; size reduction, washing, removal of hair from hides and degreasing are necessary to
prepare the hides and skins for the main extraction step.
Collagen hydrolysis is performed by one of three different methods: acid, alkali, and enzymatic
hydrolysis. Acid treatment is especially suitable for less fully crosslinked materials such as pig skin
collagen and normally requires 10 to 48 hours. Alkali treatment is suitable for more complex collagen
such as the collagen found in bovine hides and requires more time, normally several weeks. The purpose
of the alkali treatment is to destroy certain chemical crosslinkages still present in collagen. Within the
gelatin industry, the gelatin obtained from acidtreated raw material has been called typeA gelatin and
the gelatin obtained from alkalitreated raw material is referred to as typeB gelatin.[6]
Enzymatic hydrolysis of collagen for gelatin extraction is relatively new. However, the treatment time is
shorter than that required for alkali treatment, and results in almost complete conversion to the pure
product. The physical properties of the final gelatin product are better.
Extraction
After preparation of the raw cool material, i.e., reducing crosslinkages between collagen components
and removing some of the impurities such as fat and salts, partially purified collagen is converted into
gelatin by extraction with either water or acid solutions at appropriate temperatures. All industrial
processes are based on neutral or acid pH values because though alkali treatments speed up conversion,
they also promote degradation processes. Acidic extraction conditions are extensively used in the
industry but the degree of acid varies with different processes. This extraction step is a multistage
process, and the extraction temperature is usually increased in later extraction steps. This procedure
ensures the minimum thermal degradation of the extracted gelatin.
Recovery
This process includes several steps such as filtration, evaporation, drying, grinding, and sifting. These
operations are concentrationdependent and also dependent on the particular gelatin used. Gelatin
degradation should be avoided and minimized, therefore the lowest temperature possible is used for the
recovery process. Most recoveries are rapid, with all of the processes being done in several stages to
avoid extensive deterioration of the peptide structure. A deteriorated peptide structure would result in a
low gelling strength, which is not generally desired.
http://en.wikipedia.org/wiki/Gelatin
3/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
Uses
Culinary uses
Probably best known as a gelling agent in cooking, different
types and grades of gelatin are used in a wide range of food and
nonfood products: Common examples of foods that contain
gelatin are gelatin desserts, trifles, aspic, marshmallows, candy
corn, and confections such as Peeps, gummy bears, fruit snacks,
and jelly babies. Gelatin may be used as a stabilizer, thickener, or
texturizer in foods such as yogurt, cream cheese, and margarine;
it is used, as well, in fatreduced foods to simulate the mouthfeel
of fat and to create volume without adding calories.
Eggs in aspic
Gelatin is used for the clarification of juices, such as apple juice,
and of vinegar. Isinglass, from the swim bladders of fish, is still
used as a fining agent for wine and beer.[7] Beside hartshorn jelly, from deer antlers (hence the name
"hartshorn"), isinglass was one of the oldest sources of gelatin.
Technical uses
Certain professional and theatrical lighting equipment use
colour gels to change the beam colour. These were
historically made with gelatin, hence the term colour gel.
Gelatin typically constitutes the shells of pharmaceutical
capsules in order to make them easier to swallow.
Hypromellose is a vegetarianacceptable alternative to
gelatin, but is more expensive to produce.
Animal glues such as hide glue are essentially unrefined
gelatin.
It is used to hold silver halide crystals in an emulsion in
Capsules made of gelatin.
virtually all photographic films and photographic papers.
Despite some efforts, no suitable substitutes with the stability and low cost of gelatin have been
found.
Used as a carrier, coating or separating agent for other substances; for example, it makes beta
carotene watersoluble thus imparting a yellow colour to any soft drinks containing betacarotene.
Gelatin is closely related to bone glue and is used as a binder in match heads and sandpaper.
Cosmetics may contain a nongelling variant of gelatin under the name hydrolyzed collagen.
Gelatin was first used as an external surface sizing for paper in 1337 and continued as a dominant
sizing agent of all European papers through the mid19th century.[8] In modern times it
occasionally found in some glossy printing papers, artistic papers, playing cards, and it maintains
the wrinkles in crêpe paper.
http://en.wikipedia.org/wiki/Gelatin
4/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
Other uses
Blocks of ballistic gelatin simulate muscle tissue as a standardized medium for testing firearms
ammunition.
Gelatin is used by synchronized swimmers to hold their hair in place during their routines as it
will not dissolve in the cold water of the pool. It is frequently referred to as "knoxing," a reference
to Knox brand gelatin.[9]
When added to boiling water and cooled, unflavored gelatin can make a homemade hair styling
gel that is cheaper than many commercial hair styling products, but by comparison has a shorter
shelf life (about a week) when stored in this form (usually in a refrigerator). After being applied to
scalp hair, it can be removed with rinsing and some shampoo.
It is commonly used as a biological substrate to culture adherent cells.
It may be used by those who are sensitive to tannins (which can irritate the stomach) in teas, soups
or brews.
It may be used as a medium with which to consume LSD. LSD in gelatin form is known as
"windowpane" or "geltabs."
Gelatin is used to make the shells of paintballs, similar to the way pharmaceutical capsules are
produced.
Gelatin is used as an ingredient in implantable medical devices, such as in some bone void fillers.
Gelatin is used in nail polish remover and makeup applications. The gelatin is often tinted in
different colours to match a model's natural skin tone.
Leaf or sheet gelatin is used directly in foodbased modelmaking, for example to make
translucent, edible, diamondpaned windows in gingerbread houses.[10]
Gelatin can be used as a binding agent in india ink.
Gelatin may be used as a technique within the process of fine art printmaking. The prints are made
by creating a block of gelatin and applying printing inks. The gelatin is made using twice the
normal amount of gelatin granules to the usual amount of water. Once set printmaking ink
(usually water based) is applied to its surface. Other water based media may also be applied. Items
such as dried grass, leaves and paper stencils are placed onto the inked surface. Gelatin monotype
is best done with the use of medium to lightweight paper. This is gently pressed onto the inked
plate once the 'design' has been composed.
Dietary restrictions and gelatin substitutes
The consumption of gelatin from particular animals may be forbidden by religious or cultural rules. For
example, Jewish kosher and Islamic Halal customs require gelatin from sources other than pigs, like
cows and/or fish and from animals slaughtered ritually. Romani people are cautious of gelatin products
that may have been made from horses, as their culture forbids the consumption of horses. There are
companies that specify the source of the gelatin used. Vegans and many vegetarians choose not to eat
foods containing gelatin made from animals. Likewise, Hindu & Jain customs may require gelatin
http://en.wikipedia.org/wiki/Gelatin
5/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
alternatives from sources other than animals, as many Hindus are vegetarian. Hindus who are not
vegetarians will often consume gelatin from all sources except cow, which is considered sacred. Other
people simply consider gelatin unpalatable due to the ingredients used in its production.
Partial, nonanimal alternatives to gelatin include the seaweed extracts agar and carrageenan, as well as
pectin and konjak. Research into synthetic collagen is ongoing, as of 2011 partial success has been
achieved in replicating collagen's structure using selfassembling peptides.[11]
Medical and nutritional properties
Although gelatin is 9899% protein by dry weight, it has less
nutritional value than many other complete protein sources.
Gelatin is unusually high in the nonessential amino acids
glycine and proline (i.e., those produced by the human body),
while lacking certain essential amino acids (i.e., those not
produced by the human body). It contains no tryptophan and is
deficient in isoleucine, threonine, and methionine. The
approximate amino acid composition of gelatin is: glycine 21%,
proline 12%, hydroxyproline 12%, glutamic acid 10%, alanine
9%, arginine 8%, aspartic acid 6%, lysine 4%, serine 4%, leucine
3%, valine 2%, phenylalanine 2%, threonine 2%, isoleucine 1%,
Amino acid composition
hydroxylysine 1%, methionine and histidine <1% and tyrosine
<0.5%. These values vary, especially the minor constituents,
depending on the source of the raw material and processing technique.[12]
Gelatin is also a topical haemostatic. A piece of gelatin sponge of appropriate size is applied on bleeding
wound, pressed for some time and tied in bandage. Haemostatic action is based on platelets damage at
the contact of blood with gelatin, which activates the coagulation cascade. Gelatin also causes a
tamponading effect blood flow stoppage into a blood vessel by a constriction of the vessel by an
outside force.[13]
It has been claimed that oral gelatin consumption has a beneficial therapeutic effect on hair loss in both
men and women.[14][15][16][17][18][19][20][21]In addition there are scientific publications that present
evidence that consumption of oral gelatin has beneficial effect for some fingernail changes and
diseases.[22][23][24][25]
Safety concerns
Strict regulations apply for all steps in the gelatin manufacturing process. Gelatin is produced from
natural raw materials which originate from animals that have been examined and accepted for human
consumption by veterinary authorities. Hygienic regulations with respect to fresh raw materials are
ensured and each batch of raw material delivered to the manufacturing plant is immediately checked and
documented.
In addition to the raw material quality, the production process itself is an effective quality assurance
measure. In the production process a comprehensive monitoring system ensures that potential risks are
minimized.
http://en.wikipedia.org/wiki/Gelatin
6/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
The U.S. Food and Drug Administration (FDA), with support from the TSE (Transmissible spongiform
encephalopathy) Advisory Committee, has since 1997 been monitoring the potential risk of transmitting
animal diseases, especially bovine spongiform encephalopathy (BSE), commonly known as Mad Cow
disease. The FDA study concluded: "...steps such as heat, alkaline treatment, and filtration could be
effective in reducing the level of contaminating TSE agents; however, scientific evidence is insufficient
at this time to demonstrate that these treatments would effectively remove the BSE infectious agent if
present in the source material."[26]
The Scientific Steering Committee (SSC) of the European Union (EU) in 2003 stated that the risk
associated with bovine bone gelatin is very low or zero.[27][28] In 2006 the European Food Safety
Authority (EFSA) stated that the SSC opinion was confirmed, that the BSE risk of bonederived gelatin
was very small, and removed support for the 2003 request of excluding the skull and vertebrae of bovine
origin older than 12 months from the material used in gelatin manufacturing.[29]
All reputable gelatin manufacturers today follow the Quality Management System according to ISO
9001. In this way all process steps are documented. For pharmaceutical grade gelatins strict regulations
from the Food and Drug Administration (FDA), the European CPMP's regulation and European
Pharmacopoeia must be met. A detailed overview of the regulatory requirements for gelatin production
can be found in the Gelatine Handbook, pp. 99–101.[30]
References
1. ^ a b Ward, A.G.; Courts, A. (1977). The Science and Technology of Gelatin. New York: Academic Press.
ISBN 0127350500.
2. ^ a b Cole, CGB (2000), "Gelatin", in Francis, FJ, Encyclopedia of Food Science and Technology, 2nd
edition, John Wiley & Sons, pp. 1183–1188
3. ^ "Gelatine information, news, history and more" (http://www.gelatingmia.com/html/qanda.html). Gelatine
Manufacturers Institute of America. Retrieved 20080926.
4. ^ "Rousselot.com. Gelatin, Hydrolyzed collagen. Properties, processes, applications in the confectionnery,
dairy, pharmaceutical. Now is mostly used from plants industries" (http://www.rousselot.com).
ROUSSELOT. Retrieved 20080715.
5. ^ "Gelita.com" (http://www.gelita.com). GELITA Group. Retrieved 20061204.
6. ^ "Type A & B Process Definition" (http://www.vyse.com/about_gelatin_process.html). Vyse Gelatin
Company. 26 October 2009. Retrieved 16 July 2014.
7. ^ "National Organic Standards Board Technical Advisory Panel Review: Gelatin processing"
(http://www.omri.org/GelatinTAP.pdf) (PDF).
8. ^ Thurn, Jim. "History, Chemistry, and Long Term Effects of AlumRosin Size in Paper"
(https://pacer.ischool.utexas.edu/html/2081/1396/jthurn03alum.html).
9. ^ "2008 United States Olympic Synchronized Swimming Team"
(http://www.usasynchro.org/athletes/National/2008/Synchro_MediaGuide_2008.pdf) (PDF).
10. ^ "Gingerbread House Windows" (http://www.gingerbreadhouseheaven.com/gingerbreadhouse
windows.html).
11. ^ "New Method to Grow Synthetic Collagen Unveiled: New Material May Find Use in Reconstructive
Surgery, Cosmetics, Tissue Engineering"
(http://www.sciencedaily.com/releases/2011/09/110908124507.htm).
http://en.wikipedia.org/wiki/Gelatin
7/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
12. ^ Stevens, P.V. (1992). "Unknown" (http://www.gelatin.co.za/gltn1.html). Food Australia 44 (7): 320–324.
Retrieved 20050811.
13. ^ Денисенко, Петр Прокофьевич (2003). Современные лекарственные средства: Клинико
фармакологический справочник, Петр Прокофьевич Денисенко (http://books.google.com/books?
id=KoALc2Rh0IC&printsec=frontcover). ISBN 9785765427385.
14. ^ Morganti P., Randazzo S.D., Bruno C, (1982) "effect of gelatin cysteine on hair after a three months
treatment" J. Soc. Cosmet. Chemists 33, 95.
15. ^ Randazzo S.D., Morganti P., (1982) "The influence of gelatin cysteine supplementation on the amino acids
composition of human hair", accepted for presentation on XVI intern. Congress of Dermatology May 23–28
Tokyo.
16. ^ Morganti P., Bruno C. Colelli G (1983) Geltina cistina. Cheratogenesi e struttura pilifcra Boil, Soc, It.
Biol Sper 59:20.
17. ^ M.P DE Padova, A. TOSTI, Gelatin Cyctine in Seborrheic Alopecia, department of dermatology
university of Bologna – Italy, February 15, 1985. J Appl. Cosmetol 1968;4;5560 (April/June 1986).
18. ^ Titled: “Low dosage retinol and Lcystine combination improve alopecia of the diffuse type, following long
term oral administration”. By Hertel H, Gollnick H, Matthies C, Baumann I, Orfanos CE. Universitäts
Hautklinik und Poliklinik, Freien Universität Berlin. Hautarzt. 1989 Aug;40(8):4905.
19. ^ Morganti P., G. Fabrizl. B james, C. Bruno, titled: "Effect of gelatincystine and serenoa repens extract on
free radicals level and hair growth". Presented at Singapore clinical dermatology 200 – Singapore 18–20 June
1998.
20. ^ Dr. Zeev Pam, dermatologist presented a lecture titled: "Low dosage gelatin based treatments with single
dose, daily, for minimum of 36 months in female pattern hair loss." Presented at the first International
Annual Convention on the advance in hair research of the Israeli Society of Dermatology and Venereology at
the Technion, faculty of medicine, Israel, in June 2010. www.drzeevpam.com
21. ^ Dr. Nadav Pam, defended successfully the diploma work on April 2011 – “Therapeutic Effect of Gelatin as
a Dietary Supplement for Female Hair Loss”, tutored by Norbert M. Wikonkál, M.D., Ph.D at the department
of Dermatology, Venereology and Skin Oncology, Semmelweis University, Budapest, Hungary. No.
T000538/F162573. AA187105/06.11. The above mentioned diploma work was presented as a poster in the
15th Annual Meeting of the European Hair Research Society (EHRS), Jerusalem, Israel, and July 6–9, 2011
22. ^ Effect of Gelatin On the Vascularity of the Finger. Mulinos, Michael G.; Kadison, Ellen D. Angiology ,
Volume 16 (4): 170. SAGE – Apr 1, 1965.
23. ^ The Effect of Gelatin on Fragile Finger Nails by Terence Lloyd Tyson MD, The Journal of Investigative
Dermatology (1950) 14, 323–325; doi:10.1038/jid.1950.4.
24. ^ New Aspects Of The Effects Of Gelatin On Fingernails by Joseph N. Michelson, Ph. D. and David J.
Huntsman, B.S*, *applied Biological Sciences Laboratories, Inc, Glendale 1, Calif. Published in The Journal
of the society of cosmetics chemists pages 443454, May 2, 1963.
25. ^ Gelatin therapy in onychomycoses, by Jank M. Published in German language in Wien.
www.ncbi.nlm.nih.gov/pubmed/4235220. Med Wochenschr. 1968 Feb 24;118(8):1546.
26. ^ U.S. Food and Drug Administration. "The Sourcing and Processing of Gelatin to Reduce the Potential Risk
Posed by Bovine Spongiform Encephalopathy (BSE) in FDARegulated Products for Human Use"
(http://www.fda.gov/RegulatoryInformation/Guidances/ucm125182.htm).
27. ^ The Scientific Steering Committee (6–7 March 2003). "Updated Opinion On The Safety With Regard To
TSE Risks Of Gelatine Derived From Ruminant Bones or Hides"
(http://ec.europa.eu/food/fs/sc/ssc/out321_en.pdf).
http://en.wikipedia.org/wiki/Gelatin
8/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
28. ^ Gelatine Manufacturers of Europe (GME) (June 2003). "The Removal and Inactivation of Potential TSE
Infectivity by the Different Gelatin Manufacturing Processes"
(http://www.fda.gov/OHRMS/DOCKETS/AC/03/briefing/3969B1_1d.pdf).
29. ^ Scientific Panel on Biological Hazards of the European Food Safety Authority (EFSA) (18 January 2006).
"Quantitative assessment of the human BSE risk posed by gelatine with respect to residual BSE risk"
(http://www.efsa.europa.eu/EFSA/Scientific_Opinion/biohaz_op_ej312_qra_gelatine_summary_en1.pdf).
30. ^ Herbert Gareis; Reinhard Schrieber (2007). Gelatine Handbook: Theory and Industrial Practice. Weinheim:
WileyVCH. ISBN 3527315489.
Retrieved from "http://en.wikipedia.org/w/index.php?
title=Gelatin&oldid=640661994"
Wikimedia Commons has
media related to Gelatin.
Categories: Animal products Edible thickening agents Proteins Excipients
Conservation and restoration materials
This page was last modified on 2 January 2015 at 15:12.
Text is available under the Creative Commons AttributionShareAlike License; additional terms
may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a
registered trademark of the Wikimedia Foundation, Inc., a nonprofit organization.
http://en.wikipedia.org/wiki/Gelatin
9/9
Gelatin Wikipedia, the free encyclopedia
Gelatin
From Wikipedia, the free encyclopedia
Gelatin or gelatine (from Latin: gelatus meaning "stiff",
"frozen") is a translucent, colourless, brittle (when dry),
flavourless foodstuff, derived from collagen obtained from
various animal byproducts. It is commonly used as a gelling
agent in food, pharmaceuticals, photography, and cosmetic
manufacturing. Substances containing gelatin or functioning in a
similar way are called gelatinous. Gelatin is an irreversibly
hydrolyzed form of collagen. It is found in most gummy candy as
well as other products such as marshmallows, gelatin dessert, and
some ice cream, dip and yogurt. Household gelatin comes in the
form of sheets, granules, or powder. Instant types can be added to
the food as they are; others need to be soaked in water
beforehand.
'Sheet' or 'leaf' gelatin for cooking
Contents
1 Composition and properties
2 Production
2.1 Pretreatments
2.2 Extraction
2.3 Recovery
3 Uses
3.1 Culinary uses
3.2 Technical uses
3.3 Other uses
4 Dietary restrictions and gelatin substitutes
5 Medical and nutritional properties
6 Safety concerns
7 References
Composition and properties
Gelatin is a mixture of peptides and proteins produced by partial hydrolysis of collagen extracted from
the skin, bones, and connective tissues of animals such as domesticated cattle, chicken, pigs, and fish.
During hydrolysis, the natural molecular bonds between individual collagen strands are broken down
into a form that rearranges more easily. Its chemical composition is, in many respects, closely similar to
that of its parent collagen.[1] Photographic and pharmaceutical grades of gelatin are generally sourced
from beef bones.
http://en.wikipedia.org/wiki/Gelatin
1/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
Gelatin forms a viscous solution when dissolved in hot water, which sets to a gel on cooling. Gelatin
added directly to cold water does not dissolve well. Gelatin is also soluble in most polar solvents.
Gelatin solutions show viscoelastic flow and streaming birefringence. The solubility of the gelatin is
determined by the method of manufacture. Typically, gelatin can be dispersed in a relatively
concentrated acid. Such dispersions are stable for 10–15 days with little or no chemical changes and are
suitable for coating purposes or for extrusion into a precipitating bath.
The mechanical properties of gelatin gels are very sensitive to temperature variations, the previous
thermal history of the gel, and time. These gels exist over only a small temperature range, the upper limit
being the melting point of the gel, which depends on gelatin grade and concentration (but is typically
less than 35 °C) and the lower limit the freezing point at which ice crystallizes. The upper melting point
is below human body temperature, a factor which is important for mouthfeel of foods produced with
gelatin.[2] The viscosity of the gelatin/water mixture is greatest when the gelatin concentration is high
and the mixture is kept cool (≈ 4 °C). The gel strength is quantified using the Bloom test.
Production
The worldwide production amount of gelatin is about
375,000 metric tons per year (roughly 827 million lb). On
a commercial scale, gelatin is made from byproducts of
the meat and leather industry. Recently, fish byproducts
have also been considered because they eliminate some
of the religious obstacles surrounding gelatin
consumption.[2] Gelatin is derived from pork skins, pork,
horses, and cattle bones, or split cattle hides.[3] The raw
materials are prepared by different curing, acid, and
alkali processes which are employed to extract the dried
collagen hydrolysate. These processes[4] may take up to
several weeks, and differences in such processes have
great effects on the properties of the final gelatin
products.[5]
Gelatin can also be prepared in the home. Boiling
certain cartilaginous cuts of meat or bones will
result in gelatin being dissolved into the water.
Depending on the concentration, the resulting
stock (when cooled) will naturally form a jelly or
gel. This process is used for aspic.
While there are many processes whereby collagen
can be converted to gelatin, they all have several
factors in common. The intermolecular and
intramolecular bonds which stabilize insoluble
collagen rendering it insoluble must be broken,
and the hydrogen bonds which stabilize the
collagen helix must also be broken.[1] The
manufacturing processes of gelatin consists of three main stages:
1. Pretreatments to make the raw materials ready for the main extraction step and to remove
http://en.wikipedia.org/wiki/Gelatin
2/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
impurities which may have negative effects on physio chemical properties of the final gelatin
product,
2. The main extraction step, which is usually done with hot water or dilute acid solutions as a multi
stage extraction to hydrolyze collagen into gelatin, and finally,
3. The refining and recovering treatments including filtration, clarification, evaporation, sterilization,
drying, rutting, grinding, and sifting to remove the water from the gelatin solution, to blend the
gelatin extracted, and to obtain dried, blended and ground final product.
Pretreatments
If the raw material used in the production of the gelatin is derived from bones, dilute acid solutions are
used to remove calcium and other salts. Hot water or several solvents may be used in order to reduce the
fat content, which should not exceed 1% before the main extraction step. If the raw material consists of
hides and skin; size reduction, washing, removal of hair from hides and degreasing are necessary to
prepare the hides and skins for the main extraction step.
Collagen hydrolysis is performed by one of three different methods: acid, alkali, and enzymatic
hydrolysis. Acid treatment is especially suitable for less fully crosslinked materials such as pig skin
collagen and normally requires 10 to 48 hours. Alkali treatment is suitable for more complex collagen
such as the collagen found in bovine hides and requires more time, normally several weeks. The purpose
of the alkali treatment is to destroy certain chemical crosslinkages still present in collagen. Within the
gelatin industry, the gelatin obtained from acidtreated raw material has been called typeA gelatin and
the gelatin obtained from alkalitreated raw material is referred to as typeB gelatin.[6]
Enzymatic hydrolysis of collagen for gelatin extraction is relatively new. However, the treatment time is
shorter than that required for alkali treatment, and results in almost complete conversion to the pure
product. The physical properties of the final gelatin product are better.
Extraction
After preparation of the raw cool material, i.e., reducing crosslinkages between collagen components
and removing some of the impurities such as fat and salts, partially purified collagen is converted into
gelatin by extraction with either water or acid solutions at appropriate temperatures. All industrial
processes are based on neutral or acid pH values because though alkali treatments speed up conversion,
they also promote degradation processes. Acidic extraction conditions are extensively used in the
industry but the degree of acid varies with different processes. This extraction step is a multistage
process, and the extraction temperature is usually increased in later extraction steps. This procedure
ensures the minimum thermal degradation of the extracted gelatin.
Recovery
This process includes several steps such as filtration, evaporation, drying, grinding, and sifting. These
operations are concentrationdependent and also dependent on the particular gelatin used. Gelatin
degradation should be avoided and minimized, therefore the lowest temperature possible is used for the
recovery process. Most recoveries are rapid, with all of the processes being done in several stages to
avoid extensive deterioration of the peptide structure. A deteriorated peptide structure would result in a
low gelling strength, which is not generally desired.
http://en.wikipedia.org/wiki/Gelatin
3/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
Uses
Culinary uses
Probably best known as a gelling agent in cooking, different
types and grades of gelatin are used in a wide range of food and
nonfood products: Common examples of foods that contain
gelatin are gelatin desserts, trifles, aspic, marshmallows, candy
corn, and confections such as Peeps, gummy bears, fruit snacks,
and jelly babies. Gelatin may be used as a stabilizer, thickener, or
texturizer in foods such as yogurt, cream cheese, and margarine;
it is used, as well, in fatreduced foods to simulate the mouthfeel
of fat and to create volume without adding calories.
Eggs in aspic
Gelatin is used for the clarification of juices, such as apple juice,
and of vinegar. Isinglass, from the swim bladders of fish, is still
used as a fining agent for wine and beer.[7] Beside hartshorn jelly, from deer antlers (hence the name
"hartshorn"), isinglass was one of the oldest sources of gelatin.
Technical uses
Certain professional and theatrical lighting equipment use
colour gels to change the beam colour. These were
historically made with gelatin, hence the term colour gel.
Gelatin typically constitutes the shells of pharmaceutical
capsules in order to make them easier to swallow.
Hypromellose is a vegetarianacceptable alternative to
gelatin, but is more expensive to produce.
Animal glues such as hide glue are essentially unrefined
gelatin.
It is used to hold silver halide crystals in an emulsion in
Capsules made of gelatin.
virtually all photographic films and photographic papers.
Despite some efforts, no suitable substitutes with the stability and low cost of gelatin have been
found.
Used as a carrier, coating or separating agent for other substances; for example, it makes beta
carotene watersoluble thus imparting a yellow colour to any soft drinks containing betacarotene.
Gelatin is closely related to bone glue and is used as a binder in match heads and sandpaper.
Cosmetics may contain a nongelling variant of gelatin under the name hydrolyzed collagen.
Gelatin was first used as an external surface sizing for paper in 1337 and continued as a dominant
sizing agent of all European papers through the mid19th century.[8] In modern times it
occasionally found in some glossy printing papers, artistic papers, playing cards, and it maintains
the wrinkles in crêpe paper.
http://en.wikipedia.org/wiki/Gelatin
4/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
Other uses
Blocks of ballistic gelatin simulate muscle tissue as a standardized medium for testing firearms
ammunition.
Gelatin is used by synchronized swimmers to hold their hair in place during their routines as it
will not dissolve in the cold water of the pool. It is frequently referred to as "knoxing," a reference
to Knox brand gelatin.[9]
When added to boiling water and cooled, unflavored gelatin can make a homemade hair styling
gel that is cheaper than many commercial hair styling products, but by comparison has a shorter
shelf life (about a week) when stored in this form (usually in a refrigerator). After being applied to
scalp hair, it can be removed with rinsing and some shampoo.
It is commonly used as a biological substrate to culture adherent cells.
It may be used by those who are sensitive to tannins (which can irritate the stomach) in teas, soups
or brews.
It may be used as a medium with which to consume LSD. LSD in gelatin form is known as
"windowpane" or "geltabs."
Gelatin is used to make the shells of paintballs, similar to the way pharmaceutical capsules are
produced.
Gelatin is used as an ingredient in implantable medical devices, such as in some bone void fillers.
Gelatin is used in nail polish remover and makeup applications. The gelatin is often tinted in
different colours to match a model's natural skin tone.
Leaf or sheet gelatin is used directly in foodbased modelmaking, for example to make
translucent, edible, diamondpaned windows in gingerbread houses.[10]
Gelatin can be used as a binding agent in india ink.
Gelatin may be used as a technique within the process of fine art printmaking. The prints are made
by creating a block of gelatin and applying printing inks. The gelatin is made using twice the
normal amount of gelatin granules to the usual amount of water. Once set printmaking ink
(usually water based) is applied to its surface. Other water based media may also be applied. Items
such as dried grass, leaves and paper stencils are placed onto the inked surface. Gelatin monotype
is best done with the use of medium to lightweight paper. This is gently pressed onto the inked
plate once the 'design' has been composed.
Dietary restrictions and gelatin substitutes
The consumption of gelatin from particular animals may be forbidden by religious or cultural rules. For
example, Jewish kosher and Islamic Halal customs require gelatin from sources other than pigs, like
cows and/or fish and from animals slaughtered ritually. Romani people are cautious of gelatin products
that may have been made from horses, as their culture forbids the consumption of horses. There are
companies that specify the source of the gelatin used. Vegans and many vegetarians choose not to eat
foods containing gelatin made from animals. Likewise, Hindu & Jain customs may require gelatin
http://en.wikipedia.org/wiki/Gelatin
5/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
alternatives from sources other than animals, as many Hindus are vegetarian. Hindus who are not
vegetarians will often consume gelatin from all sources except cow, which is considered sacred. Other
people simply consider gelatin unpalatable due to the ingredients used in its production.
Partial, nonanimal alternatives to gelatin include the seaweed extracts agar and carrageenan, as well as
pectin and konjak. Research into synthetic collagen is ongoing, as of 2011 partial success has been
achieved in replicating collagen's structure using selfassembling peptides.[11]
Medical and nutritional properties
Although gelatin is 9899% protein by dry weight, it has less
nutritional value than many other complete protein sources.
Gelatin is unusually high in the nonessential amino acids
glycine and proline (i.e., those produced by the human body),
while lacking certain essential amino acids (i.e., those not
produced by the human body). It contains no tryptophan and is
deficient in isoleucine, threonine, and methionine. The
approximate amino acid composition of gelatin is: glycine 21%,
proline 12%, hydroxyproline 12%, glutamic acid 10%, alanine
9%, arginine 8%, aspartic acid 6%, lysine 4%, serine 4%, leucine
3%, valine 2%, phenylalanine 2%, threonine 2%, isoleucine 1%,
Amino acid composition
hydroxylysine 1%, methionine and histidine <1% and tyrosine
<0.5%. These values vary, especially the minor constituents,
depending on the source of the raw material and processing technique.[12]
Gelatin is also a topical haemostatic. A piece of gelatin sponge of appropriate size is applied on bleeding
wound, pressed for some time and tied in bandage. Haemostatic action is based on platelets damage at
the contact of blood with gelatin, which activates the coagulation cascade. Gelatin also causes a
tamponading effect blood flow stoppage into a blood vessel by a constriction of the vessel by an
outside force.[13]
It has been claimed that oral gelatin consumption has a beneficial therapeutic effect on hair loss in both
men and women.[14][15][16][17][18][19][20][21]In addition there are scientific publications that present
evidence that consumption of oral gelatin has beneficial effect for some fingernail changes and
diseases.[22][23][24][25]
Safety concerns
Strict regulations apply for all steps in the gelatin manufacturing process. Gelatin is produced from
natural raw materials which originate from animals that have been examined and accepted for human
consumption by veterinary authorities. Hygienic regulations with respect to fresh raw materials are
ensured and each batch of raw material delivered to the manufacturing plant is immediately checked and
documented.
In addition to the raw material quality, the production process itself is an effective quality assurance
measure. In the production process a comprehensive monitoring system ensures that potential risks are
minimized.
http://en.wikipedia.org/wiki/Gelatin
6/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
The U.S. Food and Drug Administration (FDA), with support from the TSE (Transmissible spongiform
encephalopathy) Advisory Committee, has since 1997 been monitoring the potential risk of transmitting
animal diseases, especially bovine spongiform encephalopathy (BSE), commonly known as Mad Cow
disease. The FDA study concluded: "...steps such as heat, alkaline treatment, and filtration could be
effective in reducing the level of contaminating TSE agents; however, scientific evidence is insufficient
at this time to demonstrate that these treatments would effectively remove the BSE infectious agent if
present in the source material."[26]
The Scientific Steering Committee (SSC) of the European Union (EU) in 2003 stated that the risk
associated with bovine bone gelatin is very low or zero.[27][28] In 2006 the European Food Safety
Authority (EFSA) stated that the SSC opinion was confirmed, that the BSE risk of bonederived gelatin
was very small, and removed support for the 2003 request of excluding the skull and vertebrae of bovine
origin older than 12 months from the material used in gelatin manufacturing.[29]
All reputable gelatin manufacturers today follow the Quality Management System according to ISO
9001. In this way all process steps are documented. For pharmaceutical grade gelatins strict regulations
from the Food and Drug Administration (FDA), the European CPMP's regulation and European
Pharmacopoeia must be met. A detailed overview of the regulatory requirements for gelatin production
can be found in the Gelatine Handbook, pp. 99–101.[30]
References
1. ^ a b Ward, A.G.; Courts, A. (1977). The Science and Technology of Gelatin. New York: Academic Press.
ISBN 0127350500.
2. ^ a b Cole, CGB (2000), "Gelatin", in Francis, FJ, Encyclopedia of Food Science and Technology, 2nd
edition, John Wiley & Sons, pp. 1183–1188
3. ^ "Gelatine information, news, history and more" (http://www.gelatingmia.com/html/qanda.html). Gelatine
Manufacturers Institute of America. Retrieved 20080926.
4. ^ "Rousselot.com. Gelatin, Hydrolyzed collagen. Properties, processes, applications in the confectionnery,
dairy, pharmaceutical. Now is mostly used from plants industries" (http://www.rousselot.com).
ROUSSELOT. Retrieved 20080715.
5. ^ "Gelita.com" (http://www.gelita.com). GELITA Group. Retrieved 20061204.
6. ^ "Type A & B Process Definition" (http://www.vyse.com/about_gelatin_process.html). Vyse Gelatin
Company. 26 October 2009. Retrieved 16 July 2014.
7. ^ "National Organic Standards Board Technical Advisory Panel Review: Gelatin processing"
(http://www.omri.org/GelatinTAP.pdf) (PDF).
8. ^ Thurn, Jim. "History, Chemistry, and Long Term Effects of AlumRosin Size in Paper"
(https://pacer.ischool.utexas.edu/html/2081/1396/jthurn03alum.html).
9. ^ "2008 United States Olympic Synchronized Swimming Team"
(http://www.usasynchro.org/athletes/National/2008/Synchro_MediaGuide_2008.pdf) (PDF).
10. ^ "Gingerbread House Windows" (http://www.gingerbreadhouseheaven.com/gingerbreadhouse
windows.html).
11. ^ "New Method to Grow Synthetic Collagen Unveiled: New Material May Find Use in Reconstructive
Surgery, Cosmetics, Tissue Engineering"
(http://www.sciencedaily.com/releases/2011/09/110908124507.htm).
http://en.wikipedia.org/wiki/Gelatin
7/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
12. ^ Stevens, P.V. (1992). "Unknown" (http://www.gelatin.co.za/gltn1.html). Food Australia 44 (7): 320–324.
Retrieved 20050811.
13. ^ Денисенко, Петр Прокофьевич (2003). Современные лекарственные средства: Клинико
фармакологический справочник, Петр Прокофьевич Денисенко (http://books.google.com/books?
id=KoALc2Rh0IC&printsec=frontcover). ISBN 9785765427385.
14. ^ Morganti P., Randazzo S.D., Bruno C, (1982) "effect of gelatin cysteine on hair after a three months
treatment" J. Soc. Cosmet. Chemists 33, 95.
15. ^ Randazzo S.D., Morganti P., (1982) "The influence of gelatin cysteine supplementation on the amino acids
composition of human hair", accepted for presentation on XVI intern. Congress of Dermatology May 23–28
Tokyo.
16. ^ Morganti P., Bruno C. Colelli G (1983) Geltina cistina. Cheratogenesi e struttura pilifcra Boil, Soc, It.
Biol Sper 59:20.
17. ^ M.P DE Padova, A. TOSTI, Gelatin Cyctine in Seborrheic Alopecia, department of dermatology
university of Bologna – Italy, February 15, 1985. J Appl. Cosmetol 1968;4;5560 (April/June 1986).
18. ^ Titled: “Low dosage retinol and Lcystine combination improve alopecia of the diffuse type, following long
term oral administration”. By Hertel H, Gollnick H, Matthies C, Baumann I, Orfanos CE. Universitäts
Hautklinik und Poliklinik, Freien Universität Berlin. Hautarzt. 1989 Aug;40(8):4905.
19. ^ Morganti P., G. Fabrizl. B james, C. Bruno, titled: "Effect of gelatincystine and serenoa repens extract on
free radicals level and hair growth". Presented at Singapore clinical dermatology 200 – Singapore 18–20 June
1998.
20. ^ Dr. Zeev Pam, dermatologist presented a lecture titled: "Low dosage gelatin based treatments with single
dose, daily, for minimum of 36 months in female pattern hair loss." Presented at the first International
Annual Convention on the advance in hair research of the Israeli Society of Dermatology and Venereology at
the Technion, faculty of medicine, Israel, in June 2010. www.drzeevpam.com
21. ^ Dr. Nadav Pam, defended successfully the diploma work on April 2011 – “Therapeutic Effect of Gelatin as
a Dietary Supplement for Female Hair Loss”, tutored by Norbert M. Wikonkál, M.D., Ph.D at the department
of Dermatology, Venereology and Skin Oncology, Semmelweis University, Budapest, Hungary. No.
T000538/F162573. AA187105/06.11. The above mentioned diploma work was presented as a poster in the
15th Annual Meeting of the European Hair Research Society (EHRS), Jerusalem, Israel, and July 6–9, 2011
22. ^ Effect of Gelatin On the Vascularity of the Finger. Mulinos, Michael G.; Kadison, Ellen D. Angiology ,
Volume 16 (4): 170. SAGE – Apr 1, 1965.
23. ^ The Effect of Gelatin on Fragile Finger Nails by Terence Lloyd Tyson MD, The Journal of Investigative
Dermatology (1950) 14, 323–325; doi:10.1038/jid.1950.4.
24. ^ New Aspects Of The Effects Of Gelatin On Fingernails by Joseph N. Michelson, Ph. D. and David J.
Huntsman, B.S*, *applied Biological Sciences Laboratories, Inc, Glendale 1, Calif. Published in The Journal
of the society of cosmetics chemists pages 443454, May 2, 1963.
25. ^ Gelatin therapy in onychomycoses, by Jank M. Published in German language in Wien.
www.ncbi.nlm.nih.gov/pubmed/4235220. Med Wochenschr. 1968 Feb 24;118(8):1546.
26. ^ U.S. Food and Drug Administration. "The Sourcing and Processing of Gelatin to Reduce the Potential Risk
Posed by Bovine Spongiform Encephalopathy (BSE) in FDARegulated Products for Human Use"
(http://www.fda.gov/RegulatoryInformation/Guidances/ucm125182.htm).
27. ^ The Scientific Steering Committee (6–7 March 2003). "Updated Opinion On The Safety With Regard To
TSE Risks Of Gelatine Derived From Ruminant Bones or Hides"
(http://ec.europa.eu/food/fs/sc/ssc/out321_en.pdf).
http://en.wikipedia.org/wiki/Gelatin
8/9
05/01/2015
Gelatin Wikipedia, the free encyclopedia
28. ^ Gelatine Manufacturers of Europe (GME) (June 2003). "The Removal and Inactivation of Potential TSE
Infectivity by the Different Gelatin Manufacturing Processes"
(http://www.fda.gov/OHRMS/DOCKETS/AC/03/briefing/3969B1_1d.pdf).
29. ^ Scientific Panel on Biological Hazards of the European Food Safety Authority (EFSA) (18 January 2006).
"Quantitative assessment of the human BSE risk posed by gelatine with respect to residual BSE risk"
(http://www.efsa.europa.eu/EFSA/Scientific_Opinion/biohaz_op_ej312_qra_gelatine_summary_en1.pdf).
30. ^ Herbert Gareis; Reinhard Schrieber (2007). Gelatine Handbook: Theory and Industrial Practice. Weinheim:
WileyVCH. ISBN 3527315489.
Retrieved from "http://en.wikipedia.org/w/index.php?
title=Gelatin&oldid=640661994"
Wikimedia Commons has
media related to Gelatin.
Categories: Animal products Edible thickening agents Proteins Excipients
Conservation and restoration materials
This page was last modified on 2 January 2015 at 15:12.
Text is available under the Creative Commons AttributionShareAlike License; additional terms
may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a
registered trademark of the Wikimedia Foundation, Inc., a nonprofit organization.
http://en.wikipedia.org/wiki/Gelatin
9/9
