Refine
Document Type
- Article (2)
Language
- English (2)
Is part of the Bibliography
- yes (2) (remove)
Keywords
- Casein micelle (1)
- Electroporation (1)
- Fat-soluble bioactive substances (1)
- Gelation (1)
- Interactions (1)
- Network structure (1)
- Patatin (1)
- Plant protein (1)
- Resistance heating (1)
- Transport system (1)
Institute
- Fakultät AuL (2)
The increased consumption of reduced-fat or non-fat products leads to a reduced intake of fat-soluble bioactive substances, such as fat-soluble vitamins. Due to their natural role as transport systems for hydrophobic substances, casein micelles (CM) might depict a viable system. The structure of CM is characterized by a lipophilic core stabilized by an electric double layer-like structure. Modification allows accessibility of the core and, therefore, the inclusion of fat-soluble bioactive substances. Well-known modifications are pH reduction and use of rennet enzyme. A completely new procedure to modify CM structure is offered by pulsed electrical fields (PEF). The principle behind PEF is called electroporation and affects the electric double layer of CM so that it is interrupted. In this way, lipophilic substances can be incorporated into CM. In this work, we evaluated integration of β-carotene into native CM by an industry-compatible process to overcome disadvantages associated with the use of Na-caseinate and avoid great technical effort, e.g., due to treatment with high hydrostatic pressure. Our research has shown that PEF can be used for disintegration of CM and that significant amounts of β-carotene can be incorporated in CM. Furthermore, after disintegration using PEF, a combination of another PEF and thermal treatment was applied to restructure CM and trap significant amounts of β-carotene, permanently, ending up with an encapsulation efficiency of 78%.
The influence of moderate electric fields (MEF) on thermally induced gelation and network structures of patatin enriched potato protein (PPI) was investigated. PPI solutions with 9 wt% protein (pH 7) and 25 mM NaCl were heated from 25 to 65 °C via OH (3–24 V/cm) or conventional heating (COV) at various come-up (240 s and 1200 s) and holding times (30 s and 600 s). Self-standing gels were produced but less proteins denatured when heated via OH. Further, SDS-PAGE and GPC measurements revealed more native patatin remaining after OH treatment. Scanning electron microscopy showed OH gels to have more gap-like structures and frayed areas than COV treated gels which resulted in lower water holding capacity. On molecular scale, less hydrophobic interactions were measured within the protein network and FTIR trials showed the MEF to affect beta-sheet structures. OH gels further showed lower rigidity and higher flexibility, thus, gelling functionality was affected via OH.