Co-expressing Rubisco activase in Rubisco-based engineered Escherichia coli for in situ CO2 recycling

碩士 === 國立中興大學 === 化學工程學系所 === 107 === Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is arguably one of the most abundant proteins in the biosphere and a key enzyme responsible for biological CO2 assimilation. However, the catalytic limitations of RuBisCO compromise the efficiency of phot...

Full description

Bibliographic Details
Main Authors: Ju-Jiun Pang, 龐竹均
Other Authors: 李思禹
Format: Others
Language:en_US
Published: 2019
Online Access:http://ndltd.ncl.edu.tw/handle/a6nqx9
Description
Summary:碩士 === 國立中興大學 === 化學工程學系所 === 107 === Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is arguably one of the most abundant proteins in the biosphere and a key enzyme responsible for biological CO2 assimilation. However, the catalytic limitations of RuBisCO compromise the efficiency of photosynthesis. RuBisCO has been shown to form inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. To maintain photosynthetic CO2 fixation a group of molecular motors known as RuBisCO activase which remodel inhibited RuBisCO complexes back to the active RuBisCO. In this study, we hope to enhance the activity of RuBisCO by RuBisCO activase (Rca) to increase the metabolic yield of the fermentation, and carbon flow regulation by the Pdc-based carbon tap valve for in situ CO2 recycling. The results of fermentation showed that the in vivo activity of RuBisCO, which can be demonstrated by increased total metabolic yield and product distribution. When the CO2 emission was only 0.08 ± 0.02, the total fermentation yield increased from 1.46±0.00 to 2.23±0.08. The result indicates that the activity of RuBisCO can maintain in the presence of RuBisCO activase (Rca) and can recover carbon dioxide in a low CO2 environment, thereby achieving in situ CO2 recycling.