Rubisco Case Study

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titel

achterkant

Voorwoord

Samenvatting

Table of Contents
List of abbreviations 1
1. Introduction 2
1.1 Biobased products 2
1.2 RuBisCO 3
1.3 Isochrysis galbana 4
1.4 Tetraselmis sp 4
2. Methods 5
2.1 Size Exclusion Chromatography 5
2.2 SDS-PAGE 6
2.3 Bradford protein assay 7
2.4 Ion Exchange Chromatography 7
2.5 Soxhlet extraction method 8
2.6 Kjeldahl method 8
3. Materials 9
3.1 Size Exclusion Chromatography 9
3.2 SDS-PAGE 9
3.3 Bradford protein assay 9
3.4 Ion Exchange Chromatography 10
3.5 Soxhlet extraction method 10
3.6 Kjeldahl method 10
3.7 Enzymatic digestion 10
3.8 Used strains 11
3.9 General protein extraction method 11
4. Results 12
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RuBisCO has a catalytic rate of a few CO2 molecules per second at 25 °C 19. Besides it has a low affinity for atmospheric CO2 and uses O2 as an alternative substrate. For these reasons RuBisCO is an inefficient enzyme as the initial CO2-fixing enzyme for photosynthesis. Therefore, plants and algae must contribute a major part of their nitrogen to RuBisCO. The total soluble protein content inside the plants can comprise up to 50%20.
Because RuBisCO is so abundantly present in plants it was assumed that the same applies to microalgae. In 1991, J.A. Raven compiled a dataset for RuBisCO in microalgae as the fraction of RuBisCO to total protein by mass, showing values between 2% and 23%. To determine these percentages however, an indirect measurement was performed where RuBisCO is converted on a total protein basis assuming the chlorophyll: total protein mass ratio is 0.0421.
Therefore, Losh et al. conducted experiments where RuBisCO was measured with Quantitative Western blots using an antibody which binds to a conserved region of the large subunit of RuBisCO. They concluded that RuBisCO represented < 6% of total protein in eight species of microalgae. Furthermore, they concluded that unlike in plants, RuBisCO does not account for a major fraction of cellular nitrogen in

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