Tuesday, October 12, 2010

About Gelatin

'Sheet' or 'leaf' gelatin for cooking
Gelatin (spelled gelatine in some Commonwealth countries, from the French gélatine) is a translucent, colorless, brittle (when dry), nearly tasteless solid substance, derived from the collagen inside animals' skin and bones. 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 calledgelatinous.
Gelatin is an irreversibly hydrolysed form of collagen, and is classified as a foodstuff, with E number E441. It is found in some gummy candies as well as other products such as marshmallows, gelatin dessert, and some low-fat 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. Some dietary or religious customs forbid the use of gelatin from certain animal sources, and medical issues may limit or prevent its consumption by certain people.

Composition and properties

Gelatin is a protein produced by partial hydrolysis of collagen extracted from the boiled bones, connective tissues, organs and some intestines of animals such as domesticated cattle,pigs, and horses. The natural molecular bonds between individual collagen strands are broken down into a form that rearranges more easily. Gelatin melts to a liquid when heated and solidifies when cooled again. Together with water, it forms a semi-solid colloid gel. Gelatin forms a solution of high viscosity in water, which sets to a gel on cooling, and its chemical composition is, in many respects, closely similar to that of its parent collagen.[1] Gelatin solutions show viscoelastic flow and streaming birefringence. If gelatin is put into contact with cold water, some of the material dissolves. 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. Gelatin is also soluble in most polar solvents. Gelatin 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 and the lower limit, the freezing point at which ice crystallizes. The mechanical properties are very sensitive to temperature variations, previous thermal history of the gel, and time. The viscosity of the gelatin/water mixture increases with concentration and when kept cool (≈ 4 °C).

Production

If the physical material that will be used in production is derived from bones, dilute acid solutions are used to remove calcium and similar salts. Hot water or several solvents may be used for degreasing. Maximum fat content of the material should not exceed 1% before the main extraction step. If the raw material is hides and skin, size reduction, washing, removing hair from the hides, and degreasing are the most important pretreatments used to make the hides and skins ready for the main extraction step. Raw material preparation for extraction is done by three different methods: acid, alkali, and enzymatic treatments. Acid treatment is especially suitable for less fully crosslinked materials such as pig skin collagen. Pig skin collagen is less complex than the collagen found in bovine hides. Acid treatment is faster than alkali treatment and normally requires 10 to 48 hours. Alkali treatment is suitable for more complex collagen, e.g., the collagen found in bovine hides. This process requires longer time, normally several weeks. The purpose of the alkali treatment is to destroy certain chemical crosslinkages still present in collagen. The gelatin obtained from acid treated raw material has been called type-A gelatin, and the gelatin obtained from alkali treated raw material is referred to as type-B gelatin. Enzymatic treatments used for preparing raw material for the main extraction step are relatively new. Enzymatic treatments have some advantages in contrast to alkali treatment. Time required for enzymatic treatment is short, the yield is almost 100% in enzymatic treatment, the purity is also higher, and the physical properties of the final gelatin product are better.

The worldwide production amount of gelatin is about 300,000 tons per year (roughly 660 million lb). On a commercial scale, gelatin is made from by-products of the meat and leather industry. Recently, fish by-products have also been considered because they eliminate some of the religious obstacles surrounding gelatin consumption [2]. Gelatin is derived mainly from pork skins, pork and cattle bones, or split cattle hides; contrary to popular belief, cheese is not used.[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 broth (when cooled) will naturally form a jelly or gel. This process, for instance, may be used for the pot-au-feu dish.

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 impurities which may have negative effects on physiochemical 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 physical material that will be used in production is derived from bones, dilute acid solutions are used to remove calcium and similar salts. Hot water or several solvents may be used for degreasing. Maximum fat content of the material should not exceed 1% before the main extraction step. If the raw material is hides and skin, size reduction, washing, removing hair from the hides, and degreasing are the most important pretreatments used to make the hides and skins ready for the main extraction step. Raw material preparation for extraction is done by three different methods: acid, alkali, and enzymatic treatments. Acid treatment is especially suitable for less fully crosslinked materials such as pig skin collagen. Pig skin collagen is less complex than the collagen found in bovine hides. Acid treatment is faster than alkali treatment and normally requires 10 to 48 hours. Alkali treatment is suitable for more complex collagen, e.g., the collagen found in bovine hides. This process requires longer time, normally several weeks. The purpose of the alkali treatment is to destroy certain chemical crosslinkages still present in collagen. The gelatin obtained from acid treated raw material has been called type-A gelatin, and the gelatin obtained from alkali treated raw material is referred to as type-B gelatin. Enzymatic treatments used for preparing raw material for the main extraction step are relatively new. Enzymatic treatments have some advantages in contrast to alkali treatment. Time required for enzymatic treatment is short, the yield is almost 100% in enzymatic treatment, the purity is also higher, and the physical properties of the final gelatin product are better.

Extraction

After preparation of the raw 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. Acid extract conditions are extensively used in the industry but the degree of acid varies with different processes. This extraction step is a multi stage 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, sterilization microbiologysterilization, drying, grinding, and sifting. These operations are concentration-dependent 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.

Uses

Capsules made of gelatin.
Probably best known as a gelling agent in cooking, different types and grades of gelatin are used in a wide range of food and non-food products: Common examples of foods that contain gelatin are gelatin desserts, trifles, aspic, marshmallows, and confectioneries such as Peeps, gummy bears and jelly babies. Gelatin may be used as a stabilizer, thickener, or texturizer in foods such as jams, yoghurt, cream cheese, and margarine; it is used, as well, in fat-reduced foods to simulate the mouthfeel of fat and to create volume without adding calories.

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.[6] Beside hartshorn jelly, from deer antlers (hence the name "hartshorn"), isinglass was one of the oldest sources of gelatin. Gelatine was used for hardening paper in Colonial times.

Technical uses
  • Certain professional lighting equipment uses color gels to change the beam color. These used to be made with gelatin, hence the term color gel.
  • Gelatin typically constitutes the shells of pharmaceutical capsules in order to make them easier to swallow. Hypromellose is a vegan-acceptable 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 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 water-soluble thus imparting a yellow colour to any soft drinks containing beta-carotene.
  • Gelatin is closely related to bone glue and is used as a binder in match heads and sandpaper.
  • Cosmetics may contain a non-gelling variant of gelatin under the name hydrolyzed collagen.
  • As a surface sizing, it smooths glossy printing papers or playing cards and maintains the wrinkles in crêpe paper.

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.[8]
  • When added to boiling water and cooled, unflavored gelatin can make a home-made 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.
  • Also 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 also used as an ingredient in implantable medical devices, such as in some bone void fillers. Doctors may discuss this with their patients in cases of religious beliefs.
  • Gelatin is also used in nail polish remover and makeup applications. The gelatin is often tinted in different colors to match the models natural skin tone.

Religion and gelatin substitutes

Special kinds of gelatin indicate the specific animal origin that was used for its production. For example, Muslim halal or Jewish kosher customs may require gelatin from sources other than pigs, from animals slaughtered ritually, or from fish. Even though Muslims can not have gelatin because it contains pig fats, there are some solutions like bovine gelatin.[citation needed] Likewise, Hindu customs may require gelatin from sources other than cow which is considered sacred, although many Hindus are vegetarian. Moreover, vegetarians and vegans may choose not to eat foods containing gelatin made from animals.
Some dietary or religious customs forbid the use of gelatin from certain animal sources, and medical issues may limit or prevent its consumption by certain people.
Alternatives to gelatin include non-animal gel sources such as agar-agar (a seaweed), carrageenan, pectin, konjak, and guar gum. However, alternative sources can be associated with health problems of their own (see for instance health concerns regarding carrageenan).

Medical and nutritional properties

Amino acid composition
Although gelatin is 98-99% protein by dry weight, it has less nutritional value than many other protein sources. Gelatin is unusually high in the non-essential 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%, 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.[9]

Safety concerns

Eggs in aspic
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, also the production process itself is an effective quality assurance measure. In the production process a comprehensive monitoring system ensures that potential risks are minimized. In USA, the 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). This study has evidence that the gelatin manufacturing process itself is an effective barrier against the proliferation of possible BSE prions. The tests were based on a worst case scenario where the raw material came from BSE-infected cattle. No BSE prions could be detected in the gelatin produced by several manufacturing methods. Injections of these gelatins into the brain of experimental animals gave no establishment of TSE diseases. 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.[14][15] In 2006 the European Food Safety Authority (EFSA) stated that the SSC opinion was confirmed, that the BSE risk of bone-derived 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.[16]

All reputable gelatin manufacturers today follow the Quality Management System according to ISO 9001 to comply with all required physical, chemical, microbiological and technical production and quality standards. In this way all process steps follow international laws and customer-specific quality parameters and are guaranteed and 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, page 99-101.[16]

References:
  1. ^ a b Ward, A.G.; Courts, A. (1977). The Science and Technology of Gelatin. New York: Academic Press. ISBN 0127350500.
  2. ^ "What is Halal?". Islamic Services of America. Retrieved 2006-12-04.
  3. ^ "Gelatine information, news, history and more". Gelatine Manufacturers Institute of America. Retrieved 2008-09-26.
  4. ^ "Rousselot.com. Gelatin, Hydrolyzed collagen. Properties, processes, applications in the confectionnery, dairy, pharmaceutical. Now is mostly used from plants industries". ROUSSELOT. Retrieved 2008-07-15.
  5. ^ "Gelita.com". GELITA Group. Retrieved 2006-12-04.
  6. ^ "National Organic Standards Board Technical Advisory Panel Review: Gelatin processing" (PDF).
  7. ^ "2008 United States Olympic Synchronized Swimming Team" (PDF).
  8. ^ Stevens, P.V. (1992). "Unknown". Food Australia 44 (7): 320–324. Retrieved 2005-08-11.
  9. ^ "What was wrong with those old "Liquid Protein" Diets". June 30, 2009.
  10. ^ http://www.waningmoon.com/nails/faq.shtml
  11. ^ "Gelatin Treats Ulcer". Medical News Today. August 22, 2006.
  12. ^ http://www.gelita.com
  13. ^ Pearson, David. "Gelatin found to reduce joint pain in athletes".
  14. ^ 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".
  15. ^ Gelatine Manufacturers of Europe (GME) (June 2003). "The Removal and Inactivation of Potential TSE Infectivity by the Different Gelatin Manufacturing Processes".
  16. ^ 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".
  17. ^ Herbert Gareis; Reinhard Schrieber (2007). Gelatine Handbook: Theory and Industrial Practice. Weinheim: Wiley-VCH. ISBN 3-527-31548-9.
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