CHARACTERIZATION AND PURIFICATION OF SUGAR BEET (BETA VULGARIS) LEAF PROTEINS

Date

2025-4-10

Author

Karakaş, Tuğba Begüm

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Plant leaves are considered potential protein sources for food applications due to their nutrient profile and large availability in agricultural waste streams. In industrialized crops, only certain parts of plants (e.g., flowers, roots, fruits) are harvested, and leaves are left as waste. These waste leaves have many tons of biomass per year. It has also been reported that these discarded leaves contain high protein levels. The sugar beet plant (Beta vulgaris) included in this study is an important leaf source worldwide and is among the ten agricultural products produced in many countries. Leaf proteins consist of both soluble and insoluble proteins. The RubisCO enzyme is the most abundant protein in the soluble part. RubisCO is a ~500 kDa complex protein comprising eight large subunits (53 kDa) and eight small subunits (14 kDa). In this study, the soluble and insoluble parts of sugar beet leaf proteins were isolated, and characterized by SDS-PAGE, spectrophotometric measurements were performed with UV-VIS Spectroscopy, protein quantification was performed using various protein assays, RubisCO and other soluble and membrane proteins were identified and relatively quantified using Mass Spectrometry (MS), RubisCO was purified using Ion Chromatography and Size-Exclusion Chromatography. In addition, bioinformatics analyses were performed to identify similar proteins among other edible green-leaf plants using sequence alignments of abundant proteins in sugar beet leaves determined by proteomics analysis.

Subject Keywords

Sugar Beet Leaf Proteins, RubisCO, Protein Purification, Proteomics, Alternative Protein Sources

URI

https://hdl.handle.net/11511/114926

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Graduate School of Natural and Applied Sciences, Thesis