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- Title
EFFECT OF MICROBIAL TRANSGLUTAMINASE ON THE FRACTIONAL PROFILE OF ETHANOL-PRECIPITATED SUNFLOWER PROTEIN ISOLATE.
- Authors
IVANOVA, P.; KALAYDZHIEV, H. R.
- Abstract
To be competitive in the food ingredient markets, the functionality of sunflower proteins must be continuously improved and designed for specific uses. The present study indicates the conditions for improvement of protein functionality by modification with transglutaminase. Sunflower meal was used as a source for preparation of an ethanol-precipitated protein isolate. A commercially available enzyme transglutaminase (Activa® WM) was used for modification of the sunflower protein isolate. The modification degree of amino groups was determined by ortho-phthalaldehyde (OPA) method. Sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE) and gel chromatography were applied for characterisation of the cross-linking process. The results show that ethanol-precipitated sunflower protein isolate is an effective substrate for transglutaminase. Both 2S albumins and 11S globulins take part in the modification process. The modification degree in modified isolate was higher than that of animal proteins. The formation of high-molecular weight protein aggregates, which are an indication of the modification process, depends on the pH and duration of the reaction. The most appropriate longevity for modification under the conditions used in our experiments (temperature 40°C) was 22 h at pH 7.0. Ethanol-precipitated sunflower protein isolate was successfully modified with transglutaminase and the new modified protein isolate can be used as a supplement for human nutrition.
- Subjects
POLYACRYLAMIDE gel electrophoresis; SUNFLOWERS; TRANSGLUTAMINASES; ALBUMINS; AMINO group; SUNFLOWER seed oil; NUTRITION; PROTEINS
- Publication
Oxidation Communications, 2021, Vol 44, Issue 3, p591
- ISSN
0209-4541
- Publication type
Article