How Does the Freezer Burn Our Food?

Schmidt, Shelly J.; Lee, Joo Won

doi:10.1111/j.1541-4329.2009.00072.x

Cited by 18 publications

(5 citation statements)

References 8 publications

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“…"Freezer burn" describes the dehydration and associated changes in color, texture, and flavor that may occur on the surface of foods during frozen storage. The dehydration is caused by sublimation of ice when the vapor pressure of ice at the surface is greater than the vapor pressure of water in the air (Schmidt & Lee, 2010). A lower storage temperature leads to lower vapor pressure, for example, the vapor pressure of ice is about 100 Pa at −20 • C, but reduces to around 4 Pa at −50 • C (Weast, 1975).…”

Section: 7mentioning

confidence: 99%

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Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Bao

Ertbjerg

Estévez

et al. 2021

Comp Rev Food Sci Food Safe

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Over the recent decades,protein oxidation in muscle foods has gained increasing research interests as it is known that protein oxidation can affect eating quality and nutritional value of meat and aquatic products. Protein oxidation occurs during freezing/thawing and frozen storage of muscle foods, leading to irreversible physicochemical changes and impaired quality traits. Controlling oxidative damage to muscle foods during such technological processes requires a deeper understanding of the mechanisms of freezing-induced protein oxidation. This review focus on key physicochemical factors in freezing/thawing and frozen storage of muscle foods, such as formation of ice crystals, freeze concentrating and macromolecular crowding effect, instability of proteins at the icewater interface, freezer burn, lipid oxidation, and so on. Possible relationships between these physicochemical factors and protein oxidation are thoroughly discussed. In addition, the occurrence of protein oxidation, the impact on eating quality and nutrition, and controlling methods are also briefly reviewed. This review will shed light on the complicated mechanism of protein oxidation in frozen muscle foods.

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Section: 7mentioning

confidence: 99%

“…Surface color of frozen beef gradually change from red to brown due to the oxidation of myoglobin to the brown colored metmyo-globin. Sublimation from the surface of frozen meat may cause small air pockets to develop, forming a honeycomb structure (Schmidt & Lee, 2010). Modern self-defrosting freezers may contribute to an increase in freezer burn.…”

Section: 7mentioning

confidence: 99%

Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Bao

Ertbjerg

Estévez

et al. 2021

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

show abstract

“…In addition to freeze concentration, freezer burn may contribute to protein oxidation. Freezer burn describes the dehydration and associated changes in colour, texture and flavour that may occur on the surface of foods during frozen storage (Schmidt & Lee, 2009). This dehydration is caused by the sublimation of ice when the vapour pressure of ice on the surface of the food is greater than that of water in the air.…”

Section: Protein Denaturation and Oxidationmentioning

confidence: 99%

Protein changes in shrimp (Metapenaeus ensis) frozen stored at different temperatures and the relation to water‐holding capacity

Bao

Wang

et al. 2021

Int J of Food Sci Tech

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To study the effects of freezing temperature on muscle proteins, shrimp (Metapenaeus ensis) were frozen stored at either −18 or −60°C up to 90 and 210 days. Shrimp frozen at −18°C had higher thawing and compression loss and poor myofibril water-holding capacity compared with those frozen at −60°C. In terms of protein characteristics, shrimp frozen at −18°C had higher levels of carbonyls and reduced sulphhydryls. Moreover, the shrimp frozen at −18°C had higher surface hydrophobicity and reduced Ca 2+ -ATPase activity, indicating increased protein denaturation. Proteomics revealed that seventy-five proteins were classified as differentially abundant proteins (DAPs) following freezing. There were sixtyfour DAPs in the F18-CON comparison group (shrimp frozen at −18°C vs. control) and thirty-two DAPs in the F60-CON comparison group (shrimp frozen at −60°C vs. control), suggesting that freezing at −18°C results in more DAPs than freezing at −60°C. A comparison between F18 and F60 revealed that ribosomal proteins (L44, L7a) and heat shock protein 21 were downregulated in F18. These results increase our understanding of the variable quality associated with shrimp frozen at different temperatures.

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“…In containers with relatively large headspace, a phenomenon akin to "freezer burn" may occur, particularly for storage at À20 C, and in freezers that are subject to frequent temperature fluctuations due to opening and closing of the doors. 92 If the product ice surface temperature rises, water vapor from the surface sublimes into the headspace and condenses and refreezes on the walls, especially as the walls may cool down faster when the temperature drops, driven by the P H2O (s) > P H2O (hs) > P H2O (w), where P is the vapor pressure of water (H 2 O) at ice surface (s), headspace (hs), and wall (w). 92 This may become especially apparent in long stability studies in vials/small bottles (see Fig.…”

Section: Significance Of Container Headspace In Storage Of Frozen Biopharmaceuticalsmentioning

confidence: 99%

Freezing of Biologicals Revisited: Scale, Stability, Excipients, and Degradation Stresses

Authelin

Rodrigues

Tchessalov

et al. 2020

Journal of Pharmaceutical Sciences

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Although many biotech products are successfully stored in the frozen state, there are cases of degradation of biologicals during freeze storage. These examples are discussed in the Perspective to emphasize the fact that stability of frozen biologicals should not be taken for granted. Frozen-state degradation (predominantly, aggregation) has been linked to crystallization of a cryoprotector in many cases. Other factors, for example, protein unfolding (either due to cold denaturation or interaction of protein molecules with ice crystals), could also contribute to the instability. As a hypothesis, additional freezingrelated destabilization pathways are introduced in the paper, that is, air bubbles formed on the ice crystallization front, and local pressure and mechanical stresses due to volume expansion during waterto-ice transformation. Furthermore, stability of frozen biologicals can depend on the sample size, via its impact on the freezing kinetics (i.e., cooling rates and freezing time) and cryoconcentration effects, as well as on the mechanical stresses associated with freezing. We conclude that, although fundamentals of freezing processes are fairly well described in the current literature, there are important gaps to be addressed in both scientific foundations of the freezing-related manufacturing processes and implementation of the available knowledge in practice.

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How Does the Freezer Burn Our Food?

Cited by 18 publications

References 8 publications

Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Protein changes in shrimp (Metapenaeus ensis) frozen stored at different temperatures and the relation to water‐holding capacity

Freezing of Biologicals Revisited: Scale, Stability, Excipients, and Degradation Stresses

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