A Saliva-Inspired Model of Enzymatic Starch Hydrolysis by Alpha Amylase
- 1Department of Physical Sciences, Indian Institute of Science Education and Research (IISER) Mohali, Sector 81, SAS Nagar, Mohali 140306, Punjab, India
Abstract
We demonstrate that the enzymatic activity of alpha-amylase (AA) can serve as an effective physicochemical trigger for membrane remodeling in giant unilamellar vesicles (GUVs). This work provides insight into how primitive protocellular reactions directly translate into the membrane's mechanical responses. Analysis of the potato starch utilized in this work is composed of ~26\% amylose and ~75\% amylopectin. Quantitative DNS analysis revealed time- and concentration-dependent accumulation of reducing sugars during starch degradation by AA. The HPLC-RID chromatograms demonstrated the synthesis of glucose, maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose, and maltoheptaose, with maltose and maltotriose as the major products. The accumulation of these soluble hydrolysis products gradually increases the osmolarity of the extracellular medium surrounding the vesicles, leading to osmotic asymmetry across the membrane. This biochemical framework provides a quantitative basis for understanding membrane deformation, curvature generation, vesicle deflation, and budding. In addition to the specific starch--α-amylase system studied here, our work uncovers a general mechanism by which external biochemical reactions control membrane shape transformations via osmotic coupling. Such enzyme-driven remodeling offers a simple yet powerful strategy for inducing dynamic structural changes in artificial cells. It may provide insight into primitive protocellular processes in which metabolic activity and membrane mechanics were inherently coupled.
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BibTeX
@misc{kudawla2026salivainspired,
title = {{A Saliva-Inspired Model of Enzymatic Starch Hydrolysis by Alpha Amylase}},
author = {R. Kudawla and S. Negi and A. Singh and D. Singh and T. Bhatia},
howpublished = {bioRxiv},
year = {2026},
month = nov,
doi = {10.64898/2026.11.03.764040},
url = {https://www.biorxiv.org/content/10.64898/2026.11.03.764040v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - A Saliva-Inspired Model of Enzymatic Starch Hydrolysis by Alpha Amylase
AU - R. Kudawla
AU - S. Negi
AU - A. Singh
AU - D. Singh
AU - T. Bhatia
PY - 2026
DA - 2026/11/03
PB - bioRxiv
DO - 10.64898/2026.11.03.764040
UR - https://www.biorxiv.org/content/10.64898/2026.11.03.764040v1
AB - We demonstrate that the enzymatic activity of alpha-amylase (AA) can serve as an effective physicochemical trigger for membrane remodeling in giant unilamellar vesicles (GUVs). This work provides insight into how primitive protocellular reactions directly translate into the membrane's mechanical responses. Analysis of the potato starch utilized in this work is composed of ~26\% amylose and ~75\% amylopectin. Quantitative DNS analysis revealed time- and concentration-dependent accumulation of reducing sugars during starch degradation by AA. The HPLC-RID chromatograms demonstrated the synthesis of glucose, maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose, and maltoheptaose, with maltose and maltotriose as the major products. The accumulation of these soluble hydrolysis products gradually increases the osmolarity of the extracellular medium surrounding the vesicles, leading to osmotic asymmetry across the membrane. This biochemical framework provides a quantitative basis for understanding membrane deformation, curvature generation, vesicle deflation, and budding. In addition to the specific starch--α-amylase system studied here, our work uncovers a general mechanism by which external biochemical reactions control membrane shape transformations via osmotic coupling. Such enzyme-driven remodeling offers a simple yet powerful strategy for inducing dynamic structural changes in artificial cells. It may provide insight into primitive protocellular processes in which metabolic activity and membrane mechanics were inherently coupled.
ER -