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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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Structures and interactions of bamboo shoot protein-shellac complexes prepared by pH-driven method.

Xiao-Li Cai¹, Yue Chen¹, Liu Liu¹

¹School of Liquor and Food Engineering, Guizhou University, 550025 Guiyang, China.

International Journal of Biological Macromolecules

|January 18, 2025

Summary

Bamboo shoot protein (BSP) was complexed with shellac (SHL) to improve its stability and functional properties. The resulting bamboo shoot protein-shellac complexes demonstrated enhanced physical, chemical, and functional characteristics.

Keywords:

Bamboo shoot protein Complex Shellac pH-driven method

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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Area of Science:

Food Science
Biomaterials Science
Protein Chemistry

Background:

Bamboo shoot processing by-products are rich in protein and essential amino acids.
Single plant proteins like bamboo shoot protein (BSP) have limited utilization due to instability and reduced bioactivity in the gastrointestinal tract.
Complexation with natural polymers can enhance the stability and functional properties of plant proteins.

Purpose of the Study:

To prepare and characterize bamboo shoot protein-shellac (BSP-SHL) complexes.
To investigate the effect of complexation on the physical, chemical, and functional properties of BSP.
To explore the potential of BSP-SHL complexes for applications requiring enhanced stability.

Main Methods:

Preparation of BSP-SHL complexes using a pH-driven method at various mass ratios.
Particle size, PDI, and zeta-potential analysis of the complexes.
Fourier-transform infrared (FTIR) spectroscopy and fluorescence intensity measurements to analyze structural changes and interactions.

Main Results:

Covalent and non-covalent interactions between BSP and SHL were observed, reducing particle size.
The BSP-SHL complex at a 2:1 ratio exhibited the smallest particle size (193.97 nm), PDI <0.20, and zeta-potential of -27.99 mV.
Complexation enhanced solution stability, thermal tolerance, and demonstrated significant inter-molecular interactions (hydrophobic, electrostatic, hydrogen bonding).

Conclusions:

The pH-driven complexation method effectively improved the stability and functional properties of bamboo shoot protein.
BSP-SHL complexes possess excellent physical, chemical, and functional characteristics, overcoming the limitations of native BSP.
These findings provide a foundation for utilizing BSP-SHL complexes, including for the loading of active compounds.