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Updated: Jun 13, 2025

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Characterization and functional properties of protein extracted from Bambusa oldhamii munro shoots
Jinlai Yang1, Jiong Zheng2, Fusheng Zhang3
1Key Laboratory of State Forestry and Grassland Administration on Bamboo Forest Ecology and Resource Utilization, China National Bamboo Research Center, Hangzhou 310012, Zhejiang, China; Long-term Observation and Research Station for Farmland Shelterbelt Ecosystem in Hangzhou-Jiaxing-Huzhou Plain, Zhejiang 310012, China.
Abstract:
Protein is rich in bamboo shoot. This study aimed to explore the physicochemical and structural characterization, and functional properties of protein (WE-BSP, SE-BSP, EE-BSP, or AE-BSP) extracted from green bamboo shoots to add its value. Pure proteins were characterized by SEM, FT-IR, Raman spectra, TGA, DSC, and amino acid analysis. The main secondary structures in the four proteins were β-turn and β-sheet. Except protein WE-BSP, there were 16 amino acids in other proteins. The functional properties of protein were conducted using fluorescence methods. Under 365 nm UV light, all of solid state proteins could emit blue fluorescence. The fluorescence intensity (409 nm, 438 nm, 450 nm) of AE-BSP decreased linearly with an increasing temperature of 30-70 °C. In the PBS buffer solution (pH = 9.18), proteins presented better fluorescence performance, and resulted with different interference capacities in the presence of a metal ion. Finally, proteins were used to image Hela cells with a concentration of 5 or 25 μg/mL, and they offered clear intracellular fluorescence in cells. Thus, the proteins extracted from natural green bamboo shoots, could be further used in cellular imaging of cancer cells.

