Studies on self‐assembly interactions of proteins and octenyl succinic anhydrate (OSA)‐modified depolymerized waxy rice starch using rheological principles
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© 2016 Wiley Periodicals, Inc. Dynamic tests (23 °C, pH - 7.0) yielding relaxation times, λ, as a function of frequency and polymer concentration were performed to assess self-assembly characteristics of biopolymers in aqueous solution. Reduction of λ-values (slope) up to a critical frequency value (CFV) helps characterize structure formation. Proteins and octenyl succinic anhydrate (OSA)-modified depolymerized waxy rice starch (DWxRc) show a well-defined λ-slope at all concentrations. Except for whey protein isolate (WPI, 0.184 g/L) and 7% OSA-modified DWxRc (1.84 g/L), the λ-values of the solutions are comparable (P > 0.05), indicating similar structures. Self-assembly interaction of α-lactalbumin (3.68 g/L) with OSA-modified polysaccharides is observed with 18.4 g/L of 7% OSA-modified DWxRc (CFV of 0.08 Hz), while WPI (3.68 g/L) exhibits self-assembly with all polysaccharides and concentrations. Transmission electron microscopy (TEM) of electrostatically precipitated proteins alone or in combination with OSA-modified polysaccharides confirms that λ-slope and CFV values relate to shape, size, and shear stability of the assembled structures.
author list (cited authors)
Puerta‐Gomez, A. F., & Castell‐Perez, M. E.