Prevention of cell rupture and juice release from meat using antifreeze proteins
- How does it work?
- What can it be used for?
- What can it not be used for?
- Related Facilities
- Further Information
|Key words||Meat juice, antifreeze protein, freezing, crystallization, cell rupture, Thawing|
How does it work?
|Primary objective||To prevent cell rupture while freezing and juice release from meat during thawing.|
|Working principle|| Biotechnological use of antifreeze and ice nucleation proteins because of their uniqueness in directly improving freezing processes.
Antifreeze proteins (AFPs) are ice structuring proteins which bind to and influence the growth of ice crystals (also called ice-structuring proteins). These proteins naturally occur in a range of species such as edible plants and fish. By using a method of isolating the protein from fish muscles the cell structure can be preserved.
The most studied glycoproteins are from two Antarctic fishes, Trematomas borgrevinki and Dissostichus mawsoni, and from a northern fish, Boreogadus saida. The most studied non-glycoprotein is from the winter flounder, P.seudopleuronectes americanus.
AFPs have no toxicological significant effects on human health.
It is obvious, that AFPs have great potential for use in a several areas especially cryopreservation and frozen foods manufacture (e.g. intrinsic AFPs in carrots affect the thermal stability of carrots after thawing)
|Additional effects||Not characterized yet for this particular product (meat).|
|Important process parameters||Thawing under pressure can be achieved at lower temperature.|
|Important product parameters||Type and amount (limit concentrations) of ice-structuring protein.|
What can it be used for?
|Products|| Various range of products containing water (ground meat, ice cream)
Useful for addition to food and could offer a new way of improving the quality of foods if they are used appropriately and become financially feasible.
|Operations|| Before freezing is started the AFPs are mixed into formulation.
Freezing, thawing, cryopreservation
|Solutions for short comings|| This data sheet replies on potential question “How to protect the frozen meat products from ice crystal separation during storage” or “How to improve the quality of frozen meat products”.
Physical damage during crystallization is avoided and crystals are prevented from further growth. Mass preparation of antifreeze protein is currently under investigation but it is considered to be very beneficial.
What can it NOT be used for?
|Products||Not specified yet.|
|Other limitations|| Concentration of AFP, if the mass can match to the selected product (from the technological point of view).
Cost of used AFP
|Risks or hazards||Very low probability of an allergic reaction can be expected.|
|Maturity|| Mass preparation of antifreeze protein is currently under investigation. Not yet used in the commercial sphere.
The glycoproteins and the winter flounder protein are available commercially but still only at costs suitable for research of specialty items. Synthetic non-glycoproteins, i.e., winter flounder cost much more than currently used synthetic methods.
|Modularity /Implementation|| The mentioned process can be inserted in an existing production line; precise method must be specified due to the type of product which is frozen.
Can be used for cryopreservation or frost protection.
|Consumer aspects|| Consumer aspects have not been specified yet.
As AFP come from fish it is not acceptable for vegetarians.
|Legal aspects|| Regulations No. 89/107/EC, 94/36/EC, 94/35/EC and 95/2/EC
Under the conditions of the Czech Republic – Notice No. 304/2004 Sb.
152/2005 Sb. and No. 431/2005 Sb., 514/2006 Sb.
|Environmental aspects||Not known.|
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|Institutes||RIGB, SEAC Unilever, DP&A Ohio University|
|References||  Nishimiya, Y., Mie, Y., Hirano, Y., Kondo, H., Miura, A., & Tsuda, S. (2008). Mass preparation and technological development of an antifreeze protein. Synthesiology, 1(1), 7-14.
 Hall-Manning, T., Spurgeon, M., Wolfreys, A. M., & Baldrick, A. P. (2004). Safety evaluation of ice-structuring protein (ISP) type III HPLC 12 preparation. lack of genotoxicity and subchronic toxicity. Food and Chemical Toxicology : An International Journal Published for the British Industrial Biological Research Association, 42(2), 321-333.
 Crevel, R. W. R., Fedyk, J. K., & Spurgeon, M. J. (2002). Antifreeze proteins: Characteristics, occurrence and human exposure. Food and Chemical Toxicology, 40(7), 899-903.
 Pertaya, N., Celik, Y., DiPrinzio, C. L., Wettlaufer, J. S., Davies, P. L., & Braslavskym P. (2007). Growth–melt asymmetry in ice crystals under the influence of spruce budworm antifreeze protein. Journal of physics: condensed matter. http://www.biophysj.org.
 Chihiro Koshimoto, Peter Mazur, Effects of warming rate, temperature, and antifreeze proteins on the survival of mouse spermatozoa frozen at an optimal rate, Cryobiology, Volume 45, Issue 1, August 2002, Pages 49-59, ISSN 0011-2240
 Bing Li and Da-Wen Sun, Novel methods for rapid freezing and thawing of foods – a review, J. of Food Engineering, Vol.54, 3, 2002, Pag. 175-182
Robert E. Feeney "Future Food Ingredients: Antifreeze Proteins". Prepared Foods, 2010.
Thawing under pressure can be achieved at lower temperature. Type and amount (limit concentrations) of ice-structuring protein. not applicable 2.2.2 chemical, biological stabilizing biotechnology Scopus: released meat juice freezing, edible antifreeze WikiSysop :Template:Review document :Template:Review status