Modification of Solubility and Heat-Induced Gelation of Amaranth 11S Globulin by Protein Engineering

• Published in: Journal of agricultural and food chemistry 2013-04, Vol.61 (14), p.3509-3516
• Main Authors: Carrazco-Peña, Laura, Osuna-Castro, Juan A, De León-Rodríguez, Antonio, Maruyama, Nobuyuki, Toro-Vazquez, Jorge F, Morales-Rueda, Juan A, Barba de la Rosa, Ana P
• Format: Article
• Language: English
• Subjects: Amaranthus - chemistry; Biological and medical sciences; Cereal and baking product industries; Dietary Proteins - chemistry; Dietary Proteins - metabolism; Dietary Supplements; differential scanning calorimetry; Food industries; food industry; Food, Formulated; functional properties; Fundamental and applied biological sciences. Psychology; gelation; Gels; globulins; Globulins - chemistry; Globulins - genetics; Globulins - metabolism; Hot Temperature; hydrophobicity; ionic strength; new products; Phase Transition; Protein Conformation; Protein Engineering; protein structure; recombinant proteins; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Seed Storage Proteins - chemistry; Seed Storage Proteins - genetics; Seed Storage Proteins - metabolism; Seeds - chemistry; Solubility; Surface Properties
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf3050999

The primary structure of amaranth 11S globulin (Ah11S) was engineered with the aim to improve its functional properties. Four continuous methionines were inserted in variable region V, obtaining the Ah11Sr+4M construction. Changes on protein structure and surface characteristics were analyzed in silico. Solubility and heat-induced gelation of recombinant amaranth 11S proglobulin (Ah11Sr and Ah11Sr+4M) were compared with the native protein (Ah11Sn) purified from amaranth seed flour. The Ah11Sr+4 M showed the highest surface hydrophobicity, but as consequence the solubility was reduced. At low ionic strength (μ = 0.2) and acidic pH (