Sunflower protein isolates chromaticity Part 2. Effect of chlorogenic acid binding on the chromaticity and available lysine content

Kratch, V. V.; Lapteva, N. A.; Alexeyeva, M. V.; Vaintraub, I. A.

doi:10.1002/food.19860300387

Cited by 3 publications

(3 citation statements)

References 11 publications

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“…The use of acid extraction for the isolation of sunflower proteins is very attractive. The sunflower seeds are characterized by a high content of o-diphenols (primarily chlorogenic acid) which at alkaline and neutral pH are oxidized and bound with proteins causing the discolouration of the latter and making them unacceptable for food use [5]. For this reason the solubility of the phytate complexes of sunflower proteins at low pH has been studied in this work.…”

Section: Introductionmentioning

confidence: 99%

The effect of phytate on the solubility of the sunflower seed proteins

Bulmaga¹,

Lapteva²,

Vaintraub³

1989

Nahrung

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11S protein of the sunflower seed is precipitated by phytate at pH 2.0, a protein‐phytate complex being formed thereby. The number of the phosphate groups bound by the time the precipitation is completed is less than one half of that of the basic groups of the 11S protein. The insolubility of the complex formed interferes with the acid extraction of protein from the sunflower meal and solvent cake. The protein extractability increases sharply after the removal of the phytate.

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Section: Introductionmentioning

confidence: 99%

The effect of phytate on the solubility of the sunflower seed proteins

Bulmaga¹,

Lapteva²,

Vaintraub³

1989

Nahrung

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“…in alkaline milieu. So, unlike the isolates obtained from sunflower meal which are discolourated by moist heat treatment [2] no darkening of the isolates obtained from the solvent-cake will be observed during their further processing.…”

Section: Resultsmentioning

confidence: 99%

“…The free and bound CA were assayed as described earlier [2]. The total CA was determined as a control test.…”

Section: Matdrials and Methodsmentioning

confidence: 99%

Changes in free and bound chlorogenic acid and in polyphenoloxidase activity during the industrial processing of sunflower seeds (Short communication)

Vaintraub¹,

Kratch²

1989

Nahrung

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Production of low chlorogenic and caffeic acid containing sunflower meal protein isolate and its use in functional wheat bread making

Shchekoldina

Aïder

2012

J Food Sci Technol

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Sunflower meal protein isolate (SMPI) is a promising food additive in different matrices. However, the uses of SMPI are limited because of the presence of antinutritional compounds like polyphenolic substances. Chlorogenic and caffeic acids are the dominants polyphenolics in the SMPI. These substances cause significant changes of the colour of the meal, proteins and food matrices during their extraction and use as food additives. Moreover, these substances lower the nutritional value of the end product due to their interaction with some amino acids such as lysine and methionine. Thus, the removal of these substances is important to enable the use of the SMPI and meal in general in a greater extent in food applications and replacing more expensive protein sources such as soy proteins. The aim of this work was to study the production of functional bread by supplementing wheat flour with sunflower meal protein isolate (SMPI). SMPI with low content of chlorogenic and caffeic acid was usefully produced following alkaline extraction and purification with succinic acid. Purified SMPI showed well balanced amino acid profile and was characterized by high water and fat absorption capacities. It was incorporated to dough formula at 8-12 % of the total wheat flour. The results showed that production of bread supplemented with SMPI was technologically feasible.The supplemented bread had high mass volume and nutritional quality compared to the control bread. The optimal SMPI to incorporate into dough formula without significant alteration of the final bread colour was established at 10 %. This study will be helpful to find economic ways to enhance the nutritional quality of wheat bread and to improve the profitability of sunflower meal residue.

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Sunflower protein isolates chromaticity Part 2. Effect of chlorogenic acid binding on the chromaticity and available lysine content

Cited by 3 publications

References 11 publications

The effect of phytate on the solubility of the sunflower seed proteins

The effect of phytate on the solubility of the sunflower seed proteins

Changes in free and bound chlorogenic acid and in polyphenoloxidase activity during the industrial processing of sunflower seeds (Short communication)

Production of low chlorogenic and caffeic acid containing sunflower meal protein isolate and its use in functional wheat bread making

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