Plant protein refers to the protein found in plant-based foods such as beans, legumes, nuts, seeds, grains, and vegetables. Unlike animal protein, which is found in meat, dairy, and eggs, plant protein is free from cholesterol and saturated fat and can be an excellent source of essential amino acids, fiber, vitamins, and minerals.
The protein folding characteristics of bacteria have been altered by a team from the Australian National University (ANU) by incorporating various elements from plant chloroplasts.
The achievement allows the researchers to examine chloroplast proteins in more depth and discover methods to improve their function more quickly, a goal that has taken 50 years to achieve.
The University of Illinois Urbana-Champaign-led project RIPE, or Realizing Improved Photosynthetic Efficiency, involves enhancing photosynthesis, the natural mechanism all plants use to turn sunlight into energy and yields, in order to make crops more productive.
RIPE is supported by the Bill & Melinda Gates Foundation, Foundation for Food & Agriculture Research, and the U.K. Foreign, Commonwealth & Development Office.
The objective of this research was to better understand and utilize Rubisco, a protein found in plant chloroplasts that starts the process of fixing atmospheric carbon dioxide into sugars during photosynthesis. Rubisco, in contrast to many other photosynthesis-related proteins, is sluggish and necessitates a multitude of ‘chaperones’ in order to function effectively.
We can now apply the protein optimization tool of Directed Evolution, a tool we have already used to speed up the CO2-fixation rates in a number of different non-plant forms, to plant Rubisco. Once we do that, we can introduce the desired changes to speed up Rubisco in crops by gene editing. Then we will see the benefits in photosynthetic performance and the impact on plant growth and yield.
Professor Whitney
Research over the last few decades has identified most, possibly all, of these partners. This gives researchers new tools for studying and accelerating the plant Rubisco in Escherichia coli, often known as E. coli, a bacteria that is commonly employed in science to analyze proteins and is prevalent in the environment, food, and human intestines.
In a new article published in the Journal of Experimental Botany, the ANU team demonstrated the utility of a robust, genetically modular, E. coli expression tool. The work builds on a comparable expression tool developed in the Manajit Hayer-Hartl lab to provide a new system better suited for improving Rubisco efficiency.
“Assembling this new bacterial bioengineering strategy and comparing its efficiency relative to natural chloroplasts was a long-term challenge,” said Whitney, a Professor in ANU’s Research School of Biology.
“Thankfully, this new technology now provides us unprecedented experimental through-put with outcomes available within days rather than the months our slow and costly traditional testing approach using plant transgenics would take.”
Whitney is sure that their discovery represents a crucial turning point in being able to tune up Rubisco activity, even if this novel E. coli Rubisco bioengineering system will require additional design adjustments to adapt its compatibility with various crops.
“We can now apply the protein optimization tool of Directed Evolution, a tool we have already used to speed up the CO2-fixation rates in a number of different non-plant forms, to plant Rubisco,” said Whitney.
“Once we do that, we can introduce the desired changes to speed up Rubisco in crops by gene editing. Then we will see the benefits in photosynthetic performance and the impact on plant growth and yield.”
