Bhattacharya Sumana, Schiavone Marc, Chakrabarti Subhra, Bhattacharya Sanjoy K
ABRD Company LLC, 1555 Wood Road, Cleveland, OH 44121, USA.
Biotechnol Appl Biochem. 2003 Oct;38(Pt 2):111-7. doi: 10.1042/BA20030060.
The enzyme carbonic anhydrase (isoform II) from bovine and human erythrocytes was immobilized using different covalent coupling methods on inert matrices. Immobilized carbonic anhydrase may enable concentration of CO2 for Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase)-catalysed fixation in bioreactors. In the present study the activity of carbonic anhydrase with respect to hydration of CO2 using soluble and immobilized enzymes was determined. The stability of the immobilization matrix, the properties of the immobilized enzymes subjected to a variation in operation variables and the activity profile with respect to storage are reported. Immobilization imparted greater thermal and storage stability and enhanced reusability.
利用不同的共价偶联方法,将来自牛和人红细胞的碳酸酐酶(同工型II)固定在惰性基质上。固定化碳酸酐酶可使二氧化碳在生物反应器中浓缩,用于由1,5-二磷酸核酮糖羧化酶/加氧酶(Rubisco)催化的固定过程。在本研究中,测定了可溶性和固定化酶催化二氧化碳水合反应的碳酸酐酶活性。报道了固定化基质的稳定性、固定化酶在操作变量变化时的性质以及储存期间的活性概况。固定化赋予了更高的热稳定性和储存稳定性,并提高了可重复使用性。