The effect of thermal denaturation on the antigenicity of glycinin

Catsimpoolas, Nicholas; Kenney, J.; Meyer, Edwin W.

doi:10.1016/0005-2795(71)90206-6

Cited by 12 publications

(8 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Loss of antigenicity is strongly associated with conformational changes involving dissociation into subunits, and reassociation of dissociates as reported by Catsimpoolas et al (1971). Fig.…”

Section: Antigenicities Of Thermal Products Of Glycinin and Fl-conglymentioning

confidence: 72%

Effects of Heat and Ionic Strength Upon Dissociation‐Association of Soybean Protein Fractions

Iwabuchi

Yamauchi

1984

Journal of Food Science

View full text Add to dashboard Cite

The effects of heat and ionic strength upon dissociation or association of soybean proteins were characterized by an immunoelectrophoresis. Among thermal products of both glycinln and p-conglycinin, the dissociated subunits of p-conglycinin retained their antigenie reactivities, while the thermal products of glycinin lost their antigenic reactivities. Appearance of immunoprecipitin arcs was dependent on the ionic strength of the solutions. This is based on the conformational changes at the ionic strengths helow 0.1 where the thermal denaturation of p-conglycinin transforms from association to dissociation. The immunoelectrophoretic results can be used to determine the ionic strength of the solution in complex systems including whole soybean extracts and soybean milk. Relationship between the differences in textural properties of tofu and conformational changes of soybean protein is discussed.

show abstract

Section: Antigenicities Of Thermal Products Of Glycinin and Fl-conglymentioning

confidence: 72%

Effects of Heat and Ionic Strength Upon Dissociation‐Association of Soybean Protein Fractions

Iwabuchi

Yamauchi

1984

Journal of Food Science

View full text Add to dashboard Cite

show abstract

“…Heating affects the immunological properties of glycinin. The antigenic properties of glycinin are retained when heated for 30 min at up to 65 °C, but are lost rapidly if heated at 70-90°C (42,43). Loss of antigenicity is associated with destruction of the quaternary structure and possibly the alteration of the secondary and tertiary structures of the individual subunits.…”

Section: Heat Denaturation At Low Protein Concentrationmentioning

confidence: 97%

“…Immunological reactivity is available for the quantitative detection of unaltered proteins retaining their quaternary structure even after denaturation (39,43,71,83). Figures 12 and 13 show the percentage of antigenicity remaining in the heattreated glycinin and /3-conglycinin solutions, respectively, as a function of ionic strength (39,77).…”

Section: Stabilizing Effect Of High Salt Concentrationmentioning

confidence: 99%

“…Antigenicity is strongly conformation dependent (78). It has been demonstrated that destruction of the quaternary structure of glycinin brings about the complete loss of antigenicity (43). Iwabuchi and Shibasaki (39,77) utilized the immunological methods to measure the unaltered glycinin and /3-conglycinin (gel electrophoretic analysis showed that they retain the quaternary structure), and determined the percentage of antigenicity that remained after heating (100°C for 5 min).…”

Section: Effect Of Ionic Strengthmentioning

confidence: 99%

See 1 more Smart Citation

Molecular understanding of heat‐induced phenomena of soybean protein

Yamauchi

Yamagishi

Iwabuchi

1991

Food Reviews International

130

View full text Add to dashboard Cite

“…The antigenicity of glycinin for antisera produced against native soyabean proteins decreases dramatically after heating to 70 to 90°C, because it presents a reduced number of epitopes available to the antibodies. 86 An approach to solving this problem is to produce anti-denatured-soyabean proteins antisera instead of antisera against native soyabean proteins. In fact, there are commercially available antibodies that enable the detection of the subunits from glycinin when heating up to 117°C.…”

Section: Immunochemical 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

View full text Add to dashboard Cite

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.

show abstract

The effect of thermal denaturation on the antigenicity of glycinin

Cited by 12 publications

References 11 publications

Effects of Heat and Ionic Strength Upon Dissociation‐Association of Soybean Protein Fractions

Effects of Heat and Ionic Strength Upon Dissociation‐Association of Soybean Protein Fractions

Molecular understanding of heat‐induced phenomena of soybean protein

Analysis of Soyabean Proteins in Meat Products: A Review

Contact Info

Product

Resources

About