Ribulose bisphosphate carboxylase/oxygenase (rubisco) from green leaves‐potential as a food protein
- 1 January 1988
- journal article
- research article
- Published by Taylor & Francis in Food Reviews International
- Vol. 4 (1) , 93-127
- https://doi.org/10.1080/87559128809540823
Abstract
Up to 25% of the total protein in green leaves consists of a single molecular species, the enzyme ribulose bisphosphate carboxylase/oxygenase (rubisco). In C3 plants rubisco molecules are found densely packed within chloroplast stroma at concentrations up to 300 mg/mL. The oligomeric protein (MW 550,000) is composed of eight large and eight small subunits which combine to form a compact, nearly spherical molecule. Rubisco is easily purified from leaf extracts in the laboratory but, as yet, there is no simple, economical method for isolating large (kilogram) quantities of the plant enzyme. The protein appears to have potential as an ingredient in animal and/or human foods. Highly purified rubisco is a tasteless, odorless, white powder with a nutritive value reported to be equal to or superior to that of other food proteins. Rubisco also possesses some desirable functional properties which might enable food processors to successfully incorporate the protein into a number of different food systems. However, much further research is needed before rubisco becomes an acceptable substitute for other animal or plant proteins.Keywords
This publication has 85 references indexed in Scilit:
- Amino acid sequence of the small subunit of d-ribulosebisphosphate carboxylase/oxygenase from nicotiana tabacumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- A role for ribulose‐1,5‐bisphosphate carboxylase as a metabolite bufferFEBS Letters, 1982
- Subunit stoichiometry of tobacco ribulose 1,5-bisphosphate carboxylaseFEBS Letters, 1980
- Leaf Fraction 1 Protein as a Nitrogen Source for the Growth of a Proteolytic Rumen BacteriumJournal of General Microbiology, 1978
- Physico-chemical studies on fraction 1 protein from alfalfa.Agricultural and Biological Chemistry, 1978
- Crystallization of Fraction I protein from tobacco by a simplified procedureFEBS Letters, 1977
- Electron microscopic studies on microcrystals of D-ribulose-1,5-biphosphate carboxylase from Dasycladus clavaeformis roth (Ag.)Biochemical and Biophysical Research Communications, 1977
- The Effects of Shade Treatment and Light Intensity on Rihulose-1,5-Diphosphate Carboxylase Activity and Fraction I Protein Level in the First Leaf of BarleyJournal of Experimental Botany, 1974
- On the average hydrophobicity of proteins and the relation between it and protein structureJournal of Theoretical Biology, 1967
- On the structural nature of fraction-I protein of rice leavesBiochemical and Biophysical Research Communications, 1965