Acetylation of amino groups and its effect on the structure of soybean glycinin.

Yamauchi, Fumio; Ono, Hidemitsu; Kamata, Yoshiro; Shibasaki, Kazuo

doi:10.1271/bbb1961.43.1309

Cited by 12 publications

(6 citation statements)

References 2 publications

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“…The results of ultracentrifugal studies of acetylated legumin are contrary to those published elsewhere for acetylated 11S globulins,16–18 where the complete dissociation of the oligomeric proteins into subunits was described. In the case of acetylated soybean glycinin the appearance of ‘polymerised’ material has been reported.…”

Section: Discussioncontrasting

confidence: 99%

“…A number of 11S globulins have therefore been investigated to elucidate the influence of acetylation upon the physicochemical properties of these proteins and to derive structure–functionality relationships. The study of acetylated soybean glycinin16 and peanut arachin17 as well as the investigation of acetylated globulins in a soybean protein isolate18 revealed a dissociation of these oligomeric proteins into their subunits. The appearance of ‘polymerised’ material besides dissociated subunits has been reported for acetylated soybean glycinin 16.…”

Section: Introductionmentioning

confidence: 99%

“…The study of acetylated soybean glycinin16 and peanut arachin17 as well as the investigation of acetylated globulins in a soybean protein isolate18 revealed a dissociation of these oligomeric proteins into their subunits. The appearance of ‘polymerised’ material besides dissociated subunits has been reported for acetylated soybean glycinin 16. The phenomenon of association or aggregation of plant globulins after acetylation has mostly been neglected.…”

Section: Introductionmentioning

confidence: 99%

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Acetylation of faba bean legumin: conformational changes and aggregation

Schwenke¹,

Knopfe²,

Seifert

et al. 2000

J. Sci. Food Agric.

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The effect of progressive acetylation upon the conformation of the 11S globulin legumin from faba bean has been studied using chemical analysis, UV, fluorescence and CD spectroscopy, viscometry and analytical ultracentrifugation. The modification did not induce complete dissociation of the oligomeric protein. Only 30% of the protein was found to be a dissociated 3S subunit after excessive acetylation, whereas 70% was a dimeric legumin aggregate with a molecular mass of about 700 kDa. The aggregation of the highly modified legumin in high‐ionic‐strength buffer solution leads to soluble higher legumin oligomers. The acetylation resulted in a moderate molecular expansion of legumin due to a changed tertiary structure, whereas the far‐UV circular dichroism spectra did not provide definitive evidence of a decrease in domain‐stabilizing β‐sheet conformations in their secondary structure. © 2000 Society of Chemical Industry

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Section: Discussioncontrasting

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Acetylation of faba bean legumin: conformational changes and aggregation

Schwenke¹,

Knopfe²,

Seifert

et al. 2000

J. Sci. Food Agric.

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“…This observation indicated that up to 45% degree of acetylation, the native chickpea proteins were initially associated to large units, but at higher degree of acetylation (49%), the associated proteins gradually dissociated to smaller units forming a less viscous dispersion, resulting in a decreased apparent viscosity and apparent yield stress. A similar observation was reported by Yamauchi and others (1979) on the investigation of acetylated glycinin using gel filtration. They showed that “polymerized” glycinin underwent drastic conformational changes in which most of the modified proteins were dissociated to smaller subunits in extensively acetylated soybean glycinin, and the apparent viscosities were greatly affected by these changes.…”

Section: Resultssupporting

confidence: 87%

Flow Properties of Acetylated Chickpea Protein Dispersions

Liu¹,

Hung²

2010

Journal of Food Science

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Chickpea protein concentrate was acetylated with acetic anhydride at 5 levels. Acetylated chickpea protein (ACP) dispersions at 3 levels (6%, 45%, and 49%) were chosen for this flow property study. Effects of protein concentration, temperature, concentrations of salt addition and particularly, degree of acetylation on these properties were examined. Compared with native chickpea proteins, the ACP dispersions exhibited a strong shear thinning behavior. Within measured temperature range (15 to 55 degrees C), the apparent viscosities of native chickpea protein dispersions were temperature independent; those of ACP dispersions were thermally affected. The flow index (n), consistency coefficient (m), apparent yield stress, and apparent viscosities of ACP dispersions increased progressively up to 45% acetylation but decreased at 49% acetylation level. Conformational studies by gel filtration suggested that chickpea proteins were associated or polymerized at up to 45% acetylation but the associated subunits gradually dissociated to smaller units at higher levels (49%) of acetylation.

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“…These specific structural features are changed by physical, chemical, or enzymatic treatments. Factors frequently studied include pH (6,7), ionic strength (8-, 10), thermal treatments (11,12), chemical modification (13,14), and enzymatic modifications (15). However, mechanical shearing has been studied relatively rarely.…”

Section: Introductionmentioning

confidence: 99%