[Spinning of rapeseed proteins]

Area of Science:

• Food Science
• Materials Science
• Biochemistry

Background:

• Understanding the rheological properties of protein mixtures is crucial for developing new food materials and fibers.
• Rapeseed globulin and casein are important plant and dairy proteins, respectively, with potential for functional applications.

Purpose of the Study:

• To investigate the rheological properties and spinnability of alkaline solutions containing mixtures of rapeseed globulin and casein.
• To determine the influence of various factors, including protein concentration, composition, temperature, and coagulant concentration, on the flow behavior and fiber characteristics.

Main Methods:

• Preparation of alkaline protein solutions with varying concentrations and ratios of rapeseed globulin and casein.
• Rheological measurements to assess plastic flow and Newtonian behavior.
• Spinnability tests and analysis of the properties of spun protein fibers.

Main Results:

• Flow behavior was significantly affected by protein concentration, globulin-casein ratio, and storage time, but not by sodium hydroxide concentration.
• Increased casein content led to more Newtonian flow.
• Spinnability and fiber properties were influenced by solution composition, protein concentration, and coagulating bath temperature, but not by sodium hydroxide or hydrochloric acid concentrations within tested ranges.
• Rapeseed albumin starchsulphate-casein mixtures showed additional dependencies on spinning solution and coagulant concentrations, with optimal properties achieved below 4% albumin starchsulphate.

Conclusions:

• The rheology and spinnability of rapeseed globulin-casein mixtures can be tailored by adjusting protein concentration and composition.
• Specific parameters of the spinning solution and coagulation bath are critical for optimizing protein fiber properties.
• Rapeseed albumin starchsulphate offers potential for modified protein fibers, but its concentration requires careful control.