Effect of acetylation on emulsifying properties of glycinin

Kim, K. S.; Rhee, Jae-Sung

doi:10.1021/jf00093a018

Cited by 22 publications

(15 citation statements)

References 20 publications

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“…ES of acylated proteins were higher than those of U-mpc in the range of pH 4-10 but lower at pH 2. A similar observation has been reported for acylated and unmodified glycinin [21]. The increase in ES with increasing pH after the isoelectric point has been attributed to the formation of charged layers around fat globules, which caused mutual repulsion and or by forming a hydrated layer around the interfacial material, which lower interfacial energy and retard droplet coalescence.…”

Section: Resultssupporting

confidence: 78%

“…Chemical derivatization through acylation of amino acid residues with acetic and succinic anhydride has been used to improve functional properties of many plant proteins including wheat [11], soybean [4], leaf protein [12], peanut [13], sunflower [14], pea [15], cotton seed [16], winged bean [17], Faba bean [18][19][20], soy glycinin [21,22], rapeseed [23][24][25], and chick pea [26]. So far, no literature is available on acylation of mucuna beans.…”

Section: Introductionmentioning

confidence: 99%

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Effect of acetylation and succinylation on solubility profile, water absorption capacity, oil absorption capacity and emulsifying properties of mucuna bean (Mucuna pruriens) protein concentrate

Lawal

Adebowale²

2004

Nahrung

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Mucuna protein concentrate was acylated with succinic and acetic anhydride. The effects of acylation on solubility, water absorption capacity, oil absorption capacity and emulsifying properties were investigated. The pH-dependent solubility profile of unmodified mucuna protein concentrate (U-mpc) showed a decrease in solubility with decrease in pH and resolubilisation at pH values acidic to isoelectric pH (pH 4). Apart from pH 2, both acetylated mucuna protein concentrates (A-mpc) and succinylated mucuna protein concentrate (S-mpc) had improved solubility over the unmodified derivative. Acylation increased the water absorption capacity (WAC) at all levels of ionic strength (0.1-1.0 M). WAC of the protein samples increased with increase in ionic strength up to 0.2 M after which a decline occurred with increase in ionic strength from 0.4-1.0 M. When protein solutions were prepared in salts of various ions, increase in WAC followed the Hofmeister series in the order: NaSCN < NaClO4 < NaI < NaBr < NaCl < Na2SO. Acetylation improved the oil absorption capacity while the lipophilic tendency reduced the following succinylation. Emulsifying capacity increased with increase in concentration up to 2, 4 and 5% w/v for U-mpc, A-mpc and S-mpc, respectively, after which an increase in concentration reduced the emulsifying capacity. Both acetylation and succinylation significantly (P < 0.05) improved the emulsifying capacity at pH 4-10. Initial increase in ionic strength up to 0.4 M for U-mpc and 0.4 M for A-mpc and S-mpc increased the emulsion capacity progressively. Further increase in ionic strength reduced emulsion capacity (EC). Contrary to the effect of various salts on WAC, increase in EC generally follows the series Na2SO4 < NaCl < NaBr < NaI < NaClO4 < NaSCN. At all levels of ionic strength studied, S-mpc had a better emulsifying activity (EA) than both A-mpc and U-mpc. EA and emulsifying stability (ES) were pH-dependent. Maximum EA and ES were recorded at pH 10. ES of protein derivatives were higher than those of U-mpc in the range of pH 4-10 but lower at pH 2. Studies revealed that both A-mpc and S-mpc had better ES and EA than the unmodified derivative when protein solutions were prepared in salts of various anions.

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Section: Resultssupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Effect of acetylation and succinylation on solubility profile, water absorption capacity, oil absorption capacity and emulsifying properties of mucuna bean (Mucuna pruriens) protein concentrate

Lawal

Adebowale²

2004

Nahrung

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“…The product can be purified by dialysis or ultrafiltration. Both succinylation and acetylation have been utilized to improve functional properties for various food proteins from sources including soybean, [8][9][10][11][12] 39 Acylation has also been used to separate protein (rapeseed and navy bean proteins) from phytic acid and to prepare low phytate isolates with good functional properties. 40 The functional properties improved by acylation include solubility, surface hydrophobicity, emulsification and fat binding capacity.…”

Section: Acylationmentioning

confidence: 99%

Modification of Food Proteins by Non-Enzymatic Methods

Shih

1992

Biochemistry of Food Proteins

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“…Acylation can improve the functionality of proteins for wider usage in the food industry (Kim and Rhee 1990;Dua and others 1996). Acylation altered the solubility of proteins such as wheat gluten (Barber and Warthesen 1982), canola isolate (Paulson and Tung 1987), and chickpea (Liu and Hung 1998).…”

Section: P Rotein Acylation Involves the Reaction Of A Nucleo-mentioning

confidence: 99%

Acylation and Solubility of Casein Precipitated by Carbon Dioxide

Santos

Tomasula

2000

Journal of Food Science

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Casein precipitated from milk using carbon dioxide (CO 2 -casein) and calcium caseinate were acetylated and succinylated. Aqueous solubility of casein was measured at pH 3, 5, 7, and 9. Acetylation extent was lower for CO 2 -casein while both succinylated to similar extents. Solubility between the unmodified caseins was similar except at pH 5 with CO 2 -casein being less soluble. Succinylation enhanced solubility for both caseins at pH 5, 7, and 9 with similar solubility between the succinylated caseins at each pH. Acetylation enhanced solubility at pH 5, however CO 2 -casein still possessed lower solubility than calcium caseinate. Acylation and solubility behavior indicated structural features in CO 2 -casein which were not present in calcium caseinate.

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Effect of acetylation on emulsifying properties of glycinin

Cited by 22 publications

References 20 publications

Effect of acetylation and succinylation on solubility profile, water absorption capacity, oil absorption capacity and emulsifying properties of mucuna bean (Mucuna pruriens) protein concentrate

Effect of acetylation and succinylation on solubility profile, water absorption capacity, oil absorption capacity and emulsifying properties of mucuna bean (Mucuna pruriens) protein concentrate

Modification of Food Proteins by Non-Enzymatic Methods

Acylation and Solubility of Casein Precipitated by Carbon Dioxide

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