Quantitative Determination of Soybean Protein in Fresh and Cooked Meat‐soy Blends

Lee, Y. B.; Rickansrud, D. A.; Hagberg, Elroy C.; Briskey, E. J.; Greaser, Marion L.

doi:10.1111/j.1365-2621.1975.tb02206.x

Cited by 42 publications

(9 citation statements)

References 10 publications

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“…After complete solubilization of the pellets and cooling, the solution was diluted with sample buffer to contain a final protein concentration of 4 mg per mL. A stacking gel electrophoresis method described by Laemmli (1970) and modified by Lee et al (1975) was employed. The final concentration of acrylamide was 3 and 10% for the upper and lower gel, respectively.…”

Section: Sds Eel Electroohoresis Sarcomere Length Measurementmentioning

confidence: 99%

Effects of Postmortem pH and Temperature Muscle Structure and Meat Tenderness

Lee

1986

Journal of Food Science

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121

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Bovine longissimus muscles with postmortem pH in the range 5.5 -7.0 were subjected to different postmortem temperatures of l", 4", 25" and 37°C. Intact beef sides with different postmortem pH were also subjected to two different environmental temperatures of 1" and 25°C. High pH muscles exhibited an extensive degradation of Z-lines, whereas low pH muscles showed a preferential degradation of M-lines and myosin heavy chains. Intermediate pH muscles did not show much degradation of muscle proteins, resulting in tougher meat than either low or high pH muscles. High postmortem temperatures enhanced the degradation of muscle proteins in excised and incubated muscle strips, but the delayed chilling of intact beef sides at 25°C for 8-hr did not affect either the structural changes or meat tenderness.

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Section: Sds Eel Electroohoresis Sarcomere Length Measurementmentioning

confidence: 99%

Effects of Postmortem pH and Temperature Muscle Structure and Meat Tenderness

Lee

1986

Journal of Food Science

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121

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“…70 With electrophoretic methods it has been possible to detect additions of soyabean proteins at levels down to 0.5%. 49,60,61,70,71 The quantitation of soyabean proteins was accomplished by Lee et al 62 in fresh and cooked samples by SDS-PAGE, using Coomassie Blue as dye and measuring the intensity of bands by densitometry. An extractability of 96% of proteins and a quantitative linear range from 10 to 115 µg soyabean proteins were achieved when the appropriate soyabean bands were considered.…”

Section: Electrophoretic Methodsmentioning

confidence: 99%

Analysis of Soyabean Proteins in Meat Products: A Review

Belloque

García

Torre

et al. 2002

Critical Reviews in Food Science and Nutrition

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The use of soyabean proteins as meat extenders has spread significantly due to the interesting nutritional and functional properties that are present in soyabean proteins. Together with these, health and economical reasons are the major causes for the addition of soyabean proteins to meat products. Nevertheless, despite the good properties associated to soyabean proteins, there are many countries in which the addition of these proteins is forbidden or in which the addition of soyabean proteins is allowed up to a certain extent. Thus, the need of analytical methods enabling the detection of added soyabean proteins in meat products is obvious. Microscopic, electrophoretic, immunologic, and chromatographic methods are the most widely used for this purpose. However, the detection of soyabean proteins in meat products presents difficulties related to the composition (meat species, meat quality, soyabean protein source, presence of other non-meat proteins, etc.) and the processing of the meat products, and, although these analytical methods have tried to overcome all these difficulties, there is still not a method enabling quantitative assessment of soyabean proteins in all kinds of meat products.

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“…Extraction of the protein can be nearly complete when heat, urea, guanidine or detergent are used in the presence of a reducing agent such as mercaptoethanol. Lee et al (22) were able to solubilize 95% of the protein in soya-beef blends, which had been heated to 100 C for 1 hr, with tris-HC1 buffer containing 3% sodium dodecylsulfate (SDS) and 1% mercaptoethanol.…”

Section: E Lectrophor Esismentioning

confidence: 99%