Behavior of Proteins at Low Temperatures

Fennema, O.

doi:10.1021/bk-1982-0206.ch006

Cited by 8 publications

(6 citation statements)

References 27 publications

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“…Due to its perishable nature (as with fish surimi), beef-heart surimi intended for extended storage will need to be frozen. Yet, a number of physical and chemical changes can occur to proteins during frozen storage, notably protein denaturation and loss of solubility (Fennema 1982;Xiong 1997). For fish surimi, the deleterious effect of freezing on the protein quality has been well established (MacDonald and Lanier 1997).…”

Section: P Reparation Of Surimi-like Protein From Animal By-mentioning

confidence: 99%

Functionality Changes in Oxidatively/Antioxidatively Washed Beef‐Heart Surimi During Frozen Storage

Parkington

Xiong

Blanchard

et al. 2000

Journal of Food Science

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Beef-heart surimi prepared using 4 washing solutions (sodium phosphate buffer alone, buffer+NaCl, buffer+propyl gallate, and buffer+sodium tripolyphosphate) and mixed with cryoprotectants was stored at -29°C and analyzed periodically up to 12 mo. All samples showed increases in gelling capacity during storage, corresponding to oxidative changes in proteins (carbonyls, hydrophobicity). Emulsifying activity of surimi, however, did not change during storage. No major differences were found between washing conditions, but propyl gallatewashed surimi tended to have the least oxidation and least increase in gel elasticity. Overall, frozen storage not only preserved the shelf life but also enhanced gelation of beef-heart surimi washed with these solutions.

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Section: P Reparation Of Surimi-like Protein From Animal By-mentioning

confidence: 99%

Functionality Changes in Oxidatively/Antioxidatively Washed Beef‐Heart Surimi During Frozen Storage

Parkington

Xiong

Blanchard

et al. 2000

Journal of Food Science

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“…From the literature it is likely that tofu and soya proteins ( Lawrence et al ., 1986 , Kanda et al ., 1992 ), fish proteins (e.g. Jarenbäck & Liljemark, 1975), alkali extracted red meat and poultry proteins ( Lawrence et al ., 1986 ), egg yolk ( Fennema, 1982) and quorn myco‐protein ( Rodger & Angold, 1991) would also be considered to be type (2) gels.…”

Section: Discussionmentioning

confidence: 99%

“…tofu, soya proteins, alkali‐extracted red meat or poultry proteins ( Lawrence et al ., 1986 ), quorn myco‐protein ( Rodger & Angold, 1991) and fish proteins ( Jarenbäck & Liljemark, 1975). Freeze‐thaw induced protein aggregation and/or gelation have also been observed in egg yolk and milk ( Fennema, 1982). In most other cases, heat, chemical treatment or dehydration are required to stabilise an ice‐induced fibre network ( Lawrence et al ., 1986 ).…”

Section: Introductionmentioning

confidence: 99%

Effects of pressure‐shift freezing and conventional freezing on model food gels

Kalichevsky-Dong¹,

Ablett

Lillford

et al. 2000

Int J of Food Sci Tech

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Gels of agar, starch, ovalbumin, gelatin and an industrial ␤-lactoglobulin protein isolate, were frozen conventionally in a Ϫ30 ЊC freezer and by pressure-shift freezing at 200 MPa at Ϫ15 ЊC. Thawing was carried out conventionally at 20 ЊC and by the application of a pressure of 200 MPa. The microscopic structure and mechanical properties of the thawed gels were compared with those of the initial gels. Microscopic examination showed that pressure-shift freezing produces smaller and more uniform ice crystal damage than conventional freezing at Ϫ30 ЊC. The results also suggest that the freeze-thaw behaviour of food gels can be categorized into two general types: (1) gels which have a reduced gel strength as a result of mechanical damage to the gel microstructure caused by ice crystal formation, and (2) gels which have an enhanced gel strength, as a result of molecular structural changes that take place in the frozen state. Agar and gelatin were found to be typical of type (1) gels, whereas starch, ␤-lactoglobulin protein isolate and ovalbumin were found to be typical of type (2) gels. In the case of starch, retrogradation during thawing was found to be the most important factor. GelatinGelatin (Sigma, type A: porcine skin ~175 bloom) gels were prepared by initially dispersing in water and then stirring at 80 ЊC for 15 minutes. The solutions were poured into aluminium coated Pressure-shift freezing of model food gels M. T. Kalichevsky-Dong et al.

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“…Con el objeto de estudiar la posible desnaturalización ocasionada por la congelación, una de las primeras propiedades analizadas fue la solubi lidad de las proteínas del músculo, estimando que cualquier alteración en la conformación de las moléculas proteicas se vería reflejada en un cambio de solubilidad. Estudios previos efectuados con distintos sistemas proteicos, que incluían desde enzimas y membranas hasta proteínas musculares, mostraron a ambos fenómenos, desnaturalización e insolubilización, estrechamente vincu lados (Hamm, 1977;Levitt, 1978;Matsumoto, 1980;Fennema, 1982).…”

Section: Propiedades De Solubilidad De Las Proteínas Del Músculounclassified

Desnaturalización de proteínas de músculo bovino durante la congelación y el almacenamiento en estado congelado

Wagner¹

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El objetivo de este trabajo de tesis es estudiar el efecto de la congelación y del almacenamiento en estado congelado sobre la desnaturalización de las proteínas del músculo bovino; y analizar la influencia que ejercen la velocidad de congelación, el tiempo y la temperatura de almacenamiento. Se propondrá una cinética de desnaturalización y de agregación de las proteínas musculares y un mecanismo de deterioro global del músculo en estado congelado. Para ello se estudiaren los siguientes parámetros indicativos de desnaturalización y agregación proteica: actividad enzimática, solubilidad, viscosidad, comportamiento reológico y electroforético, capacidad de absorción de agua y transiciones térmicas.

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Behavior of Proteins at Low Temperatures

Cited by 8 publications

References 27 publications

Functionality Changes in Oxidatively/Antioxidatively Washed Beef‐Heart Surimi During Frozen Storage

Functionality Changes in Oxidatively/Antioxidatively Washed Beef‐Heart Surimi During Frozen Storage

Effects of pressure‐shift freezing and conventional freezing on model food gels

Desnaturalización de proteínas de músculo bovino durante la congelación y el almacenamiento en estado congelado

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