Comparison of the effect of acylation and phosphorylation on surface pressure,surface potential and foaming properties of protein isolates from rapeseed (Brassica napus) |
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| Institution: | 1. Center of Research and Innovation of Myeloproliferative Neoplasms (CRIMM), Department of Experimental and Clinical Medicine, University of Florence, Florence, Italy;2. DENOTHE Excellence Center, Azienda Ospedaliera Universitaria Careggi, Florence, Italy;3. GENOMEC Doctorate School, University of Siena, Siena, Italy;4. Department of Experimental and Clinical Medicine, University of Florence, Florence, Italy;5. Center for Regenerative Medicine, Department of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy;6. Department of Experimental and Clinical Biomedical Sciences “Mario Serio,” University of Florence, Florence, Italy;1. Doctorate Institutional in Engineering and Materials Science (DICIM), Sierra Leona 530, Lomas, 2nd. Section, C.P. 78210 San Luis Potosi, San Luis Potosi, Mexico;2. Advanced Materials Research Center (CIMAV), Miguel de Cervantes # 120, Complejo Industrial Chihuahua. C.P. 31109 Chihuahua, Chih., Mexico;3. Faculty of Chemistry Sciences, Autonomous University of San Luis Potosi, Manuel Nava 6, C.P. 78290 San Luis Potosi, San Luis Potosi, Mexico;4. Faculty of Engineering, Autonomous University of San Luis Potosi, Manuel Nava 8, C.P. 78290 San Luis Potosi, San Luis Potosi, Mexico;5. Academic Coordination, Altiplano Region, Autonomous University of San Luis Potosi,Road Cedral km. 5+600, C.P. 78700 Matehuala, San Luis Potosi, Mexico;1. Department of Food Science and Technology, South China University of Technology, Guangzhou 510640, PR China;2. State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, PR China |
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| Abstract: | A protein isolate from rapeseed was exhaustively modified by acetylation, succinylation and phosphorylation. Changes in protein solubility, adsorption kinetics, surface pressure and surface potential of monolayer, wetting and foaming properties due to chemical modification were studied. Chemical modification distinctly increased the solubility of the rapeseed protein in the alkaline pH range. Acylation increased the reduction of the surface tension. An overall improved pressure transformation and increase in surface potential in monolayer after modification was observed whereby the highest changes were achieved after succinylation. The wettability with water of protein coated hydrophobic glass substrates could be improved by succinylation and phosphorylation. Chemical modification increased the foam capacity and foam expansion of the protein. A higher foam stability was only measured after acetylation and phosphorylation. Adsorption kinetics and surface potential could be related well to the properties of protein films on hydrophobic substrates as well as in foams. |
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