Bhattacharya Sumana, Schiavone Marc, Gomes James, Bhattacharya Sanjoy K
Environmental Biotechnology Division, ABRD Company LLC, 1555 Wood Road, Cleveland, OH 44121, USA.
J Biotechnol. 2004 Jul 15;111(2):203-17. doi: 10.1016/j.jbiotec.2004.04.002.
A novel scheme employing enzymatic catalysts is described enabling conversion of D-ribulose-1,5-bisphosphate (RuBP) from 3-phospho-D-glycerate (3-PGA) without loss of carbon. Bioreactors harboring immobilized enzymes namely, phosphoglycerate kinase (PGK), glycerate phosphate dehydrogenase, triose phosphate isomerase (TIM), aldolase, transketolase (TKL), phosphatase (PTASE/FP), epimerase (EMR) and phosphoribulokinase (PRK), in accordance with this novel scheme were employed. These reactors were designed and constructed based on simulations carried out to study their performance under various operational conditions and allowed production of about 56 +/- 3% RuBP from 3-PGA. This method of synthesis of RuBP from 3-PGA employing immobilized enzyme bioreactors may be used for continuous regeneration of RuBP in biocatalytic carbon dioxide fixation processes from emissions where RuBP acts as acceptor of carbon dioxide to produce 3-PGA, rendering the fixation process continuous.
描述了一种采用酶催化剂的新方案，该方案能够在不损失碳的情况下将3-磷酸-D-甘油酸（3-PGA）转化为D-核糖-1,5-二磷酸（RuBP）。根据该新方案，使用了含有固定化酶的生物反应器，这些酶包括磷酸甘油酸激酶（PGK）、磷酸甘油脱氢酶、磷酸丙糖异构酶（TIM）、醛缩酶、转酮醇酶（TKL）、磷酸酶（PTASE/FP）、差向异构酶（EMR）和磷酸核糖激酶（PRK）。这些反应器是基于模拟设计和构建的，以研究它们在各种操作条件下的性能，并能够从3-PGA中生产出约56±3%的RuBP。这种使用固定化酶生物反应器从3-PGA合成RuBP的方法可用于生物催化二氧化碳固定过程中RuBP的连续再生，在该过程中RuBP作为二氧化碳的受体生成3-PGA，使固定过程得以持续。
