A Saliva-Inspired Model of Enzymatic Starch Hydrolysis by Alpha Amylase

Alpha-amylase acting on potato starch in giant unilamellar vesicles triggers membrane remodeling, linked to time- and concentration-dependent buildup of reducing sugars and osmotic asymmetry.

• Why it matters: Primitive protocell-like reactions require a direct route from biochemistry to membrane mechanics, but quantitative links between enzyme activity and shape change are limited.
• What they did: Potato starch (~26% amylose, ~75% amylopectin) was degraded by alpha-amylase, with DNS quantifying reducing sugars and HPLC-RID identifying glucose and maltooligosaccharides.
• The result: Maltose and maltotriose dominated, and accumulating soluble products increased extracellular osmolarity, creating osmotic asymmetry that supports deformation, curvature, deflation, and budding.

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